anno_start	anno_end	anno_text	entity_type	sentence	section
24	47	in vitro reconstitution	experimental_method	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
88	93	human	species	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
94	99	PI4KB	protein	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
107	112	ACBD3	protein	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
0	34	Phosphatidylinositol 4-kinase beta	protein	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
36	41	PI4KB	protein	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
58	63	human	species	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
64	68	PI4K	protein_type	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
91	123	phosphatidylinositol 4-phosphate	chemical	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
125	129	PI4P	chemical	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
184	194	eukaryotic	taxonomy_domain	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
35	40	PI4Ks	protein_type	To convert their lipid substrates, PI4Ks must be recruited to the correct membrane compartment.	ABSTRACT
0	5	PI4KB	protein	PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown.	ABSTRACT
81	85	PI4P	chemical	PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown.	ABSTRACT
136	141	PI4KB	protein	PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown.	ABSTRACT
20	23	NMR	experimental_method	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
24	33	structure	evidence	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
52	57	PI4KB	protein	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
87	108	Golgi adaptor protein	protein_type	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
109	160	acyl-coenzyme A binding domain containing protein 3	protein	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
162	167	ACBD3	protein	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
13	18	ACBD3	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
44	49	PI4KB	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
123	128	PI4KB	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
132	137	ACBD3	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
152	170	enzymatic activity	evidence	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
184	195	ACBD3:PI4KB	complex_assembly	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
0	34	Phosphatidylinositol 4-kinase beta	protein	Phosphatidylinositol 4-kinase beta (PI4KB, also known as PI4K IIIβ) is a soluble cytosolic protein yet its function is to phosphorylate membrane lipids.	INTRO
36	41	PI4KB	protein	Phosphatidylinositol 4-kinase beta (PI4KB, also known as PI4K IIIβ) is a soluble cytosolic protein yet its function is to phosphorylate membrane lipids.	INTRO
57	66	PI4K IIIβ	protein	Phosphatidylinositol 4-kinase beta (PI4KB, also known as PI4K IIIβ) is a soluble cytosolic protein yet its function is to phosphorylate membrane lipids.	INTRO
18	23	human	species	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
24	28	PI4K	protein_type	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
56	76	phosphatidylinositol	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
78	80	PI	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
94	126	phosphatidylinositol 4-phosphate	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
128	132	PI4P	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
0	4	PI4P	chemical	PI4P is an essential lipid found in various membrane compartments including the Golgi and trans-Golgi network (TGN), the plasma membrane and the endocytic compartments.	INTRO
20	24	PI4P	chemical	In these locations, PI4P plays an important role in cell signaling and lipid transport, and serves as a precursor for higher phosphoinositides or as a docking site for clathrin adaptor or lipid transfer proteins.	INTRO
125	142	phosphoinositides	chemical	In these locations, PI4P plays an important role in cell signaling and lipid transport, and serves as a precursor for higher phosphoinositides or as a docking site for clathrin adaptor or lipid transfer proteins.	INTRO
168	176	clathrin	protein_type	In these locations, PI4P plays an important role in cell signaling and lipid transport, and serves as a precursor for higher phosphoinositides or as a docking site for clathrin adaptor or lipid transfer proteins.	INTRO
16	58	positive-sense single-stranded RNA viruses	taxonomy_domain	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
60	72	+RNA viruses	taxonomy_domain	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
109	114	human	species	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
133	138	human	species	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
139	144	PI4KA	protein	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
148	153	PI4KB	protein	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
183	187	PI4P	chemical	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
6	16	structures	evidence	These structures are essential for effective viral replication.	INTRO
45	50	viral	taxonomy_domain	These structures are essential for effective viral replication.	INTRO
26	31	PI4KB	protein	Recently, highly specific PI4KB inhibitors were developed as potential antivirals.	INTRO
0	4	PI4K	protein_type	PI4K kinases must be recruited to the correct membrane type to fulfill their enzymatic functions.	INTRO
5	12	kinases	protein_type	PI4K kinases must be recruited to the correct membrane type to fulfill their enzymatic functions.	INTRO
0	13	Type II PI4Ks	protein_type	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
15	21	PI4K2A	protein	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
26	32	PI4K2B	protein	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
38	59	heavily palmitoylated	protein_state	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
79	96	membrane proteins	protein	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
13	27	type III PI4Ks	protein_type	In contrast, type III PI4Ks (PI4KA and PI4KB) are soluble cytosolic proteins that are recruited to appropriate membranes indirectly via protein-protein interactions.	INTRO
29	34	PI4KA	protein	In contrast, type III PI4Ks (PI4KA and PI4KB) are soluble cytosolic proteins that are recruited to appropriate membranes indirectly via protein-protein interactions.	INTRO
39	44	PI4KB	protein	In contrast, type III PI4Ks (PI4KA and PI4KB) are soluble cytosolic proteins that are recruited to appropriate membranes indirectly via protein-protein interactions.	INTRO
19	24	PI4KA	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
51	55	EFR3	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
60	64	TTC7	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
164	169	PI4KB	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
0	51	Acyl-coenzyme A binding domain containing protein 3	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
53	58	ACBD3	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
74	79	GCP60	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
84	88	PAP7	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
89	98	golgin B1	protein	Its membrane localization is mediated by the interaction with the Golgi integral protein golgin B1/giantin.	INTRO
99	106	giantin	protein	Its membrane localization is mediated by the interaction with the Golgi integral protein golgin B1/giantin.	INTRO
0	5	ACBD3	protein	ACBD3 functions as an adaptor protein and signaling hub across cellular signaling pathways.	INTRO
0	5	ACBD3	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
55	64	golgin A3	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
65	75	golgin-160	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
99	112	Numb proteins	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
179	196	metal transporter	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
197	201	DMT1	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
206	215	monomeric	oligomeric_state	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
216	225	G protein	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
226	233	Dexras1	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
246	250	iron	chemical	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
272	284	lipid kinase	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
285	290	PI4KB	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
0	5	ACBD3	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
138	158	polyglutamine repeat	structure_element	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
170	176	mutant	protein_state	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
177	187	huntingtin	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
215	224	monomeric	oligomeric_state	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
225	234	G protein	protein_type	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
235	239	Rhes	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
240	247	Dexras2	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
0	5	ACBD3	protein	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
30	35	viral	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
36	62	non-structural 3A proteins	protein_type	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
92	106	picornaviruses	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
117	127	poliovirus	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
129	146	coxsackievirus B3	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
152	163	Aichi virus	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
13	56	biochemical and structural characterization	experimental_method	We present a biochemical and structural characterization of the molecular complex composed of the ACBD3 protein and the PI4KB enzyme.	INTRO
98	103	ACBD3	protein	We present a biochemical and structural characterization of the molecular complex composed of the ACBD3 protein and the PI4KB enzyme.	INTRO
120	125	PI4KB	protein	We present a biochemical and structural characterization of the molecular complex composed of the ACBD3 protein and the PI4KB enzyme.	INTRO
13	18	ACBD3	protein	We show that ACBD3 can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found.	INTRO
31	36	PI4KB	protein	We show that ACBD3 can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found.	INTRO
76	81	PI4KB	protein	We show that ACBD3 can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found.	INTRO
24	29	ACBD3	protein	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
44	62	enzymatic activity	evidence	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
66	71	PI4KB	protein	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
72	78	kinase	protein_type	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
0	5	ACBD3	protein	ACBD3 and PI4KB interact with 1:1 stoichiometry with submicromolar affinity	RESULTS
10	15	PI4KB	protein	ACBD3 and PI4KB interact with 1:1 stoichiometry with submicromolar affinity	RESULTS
44	49	ACBD3	protein	In order to verify the interactions between ACBD3 and PI4KB we expressed and purified both proteins.	RESULTS
54	59	PI4KB	protein	In order to verify the interactions between ACBD3 and PI4KB we expressed and purified both proteins.	RESULTS
63	85	expressed and purified	experimental_method	In order to verify the interactions between ACBD3 and PI4KB we expressed and purified both proteins.	RESULTS
22	42	bacterial expression	experimental_method	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
47	78	intrinsically disordered region	structure_element	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
82	87	PI4KB	protein	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
98	105	423–522	residue_range	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
111	118	removed	experimental_method	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
14	22	deletion	experimental_method	This internal deletion does not significantly affect the kinase activity(SI Fig. 1A) or interaction with ACBD3 (SI Fig. 1B,C).	RESULTS
57	63	kinase	protein_type	This internal deletion does not significantly affect the kinase activity(SI Fig. 1A) or interaction with ACBD3 (SI Fig. 1B,C).	RESULTS
105	110	ACBD3	protein	This internal deletion does not significantly affect the kinase activity(SI Fig. 1A) or interaction with ACBD3 (SI Fig. 1B,C).	RESULTS
6	28	in vitro binding assay	experimental_method	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
30	35	ACBD3	protein	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
36	74	co-purified with the NiNTA-immobilized	experimental_method	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
86	100	His6GB1-tagged	protein_state	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
101	106	PI4KB	protein	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
8	34	mammalian two-hybrid assay	experimental_method	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
60	69	localized	evidence	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
94	102	Q domain	structure_element	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
106	111	ACBD3	protein	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
152	161	glutamine	residue_name	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
180	197	N-terminal region	structure_element	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
201	206	PI4KB	protein	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
221	235	helical domain	structure_element	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
3	12	expressed	experimental_method	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
17	25	Q domain	structure_element	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
29	34	ACBD3	protein	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
45	52	241–308	residue_range	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
62	79	N-terminal region	structure_element	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
83	88	PI4KB	protein	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
99	103	1–68	residue_range	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
108	115	E. coli	species	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
34	39	ACBD3	protein	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
44	52	dimerize	oligomeric_state	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
58	84	mammalian two-hybrid assay	experimental_method	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
145	156	ACBD3:PI4KB	complex_assembly	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
4	30	sedimentation coefficients	evidence	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
34	39	ACBD3	protein	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
44	49	PI4KB	protein	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
50	55	alone	protein_state	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
60	71	ACBD3:PI4KB	complex_assembly	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
99	129	analytical ultracentrifugation	experimental_method	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
198	215	molecular weights	evidence	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
44	53	monomeric	oligomeric_state	This result suggests that both proteins are monomeric and the stoichiometry of the ACBD3: PI4KB protein complex is 1:1 (Fig. 1C, left panel).	RESULTS
83	95	ACBD3: PI4KB	complex_assembly	This result suggests that both proteins are monomeric and the stoichiometry of the ACBD3: PI4KB protein complex is 1:1 (Fig. 1C, left panel).	RESULTS
53	61	Q domain	structure_element	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
65	70	ACBD3	protein	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
79	96	N-terminal region	structure_element	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
100	105	PI4KB	protein	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
71	82	full length	protein_state	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
83	88	ACBD3	protein	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
93	98	PI4KB	protein	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
105	130	surface plasmon resonance	experimental_method	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
132	135	SPR	experimental_method	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
0	3	SPR	experimental_method	SPR measurements revealed a strong interaction with a Kd value of 320 +/−130 nM (Fig. 1D, SI Fig. 1D).	RESULTS
54	56	Kd	evidence	SPR measurements revealed a strong interaction with a Kd value of 320 +/−130 nM (Fig. 1D, SI Fig. 1D).	RESULTS
18	23	ACBD3	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
28	33	PI4KB	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
64	72	Q domain	structure_element	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
76	81	ACBD3	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
90	107	N-terminal region	structure_element	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
111	116	PI4KB	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
146	167	dissociation constant	evidence	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
0	19	Structural analysis	experimental_method	Structural analysis of the ACBD3:PI4KB complex	RESULTS
27	38	ACBD3:PI4KB	complex_assembly	Structural analysis of the ACBD3:PI4KB complex	RESULTS
0	11	Full length	protein_state	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
12	17	ACBD3	protein	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
22	27	PI4KB	protein	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
47	79	intrinsically disordered regions	structure_element	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
8	53	hydrogen-deuterium exchange mass spectrometry	experimental_method	We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis of the complex to determine which parts of the complex are well folded (SI Fig. 2).	RESULTS
55	61	HDX-MS	experimental_method	We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis of the complex to determine which parts of the complex are well folded (SI Fig. 2).	RESULTS
131	142	well folded	protein_state	We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis of the complex to determine which parts of the complex are well folded (SI Fig. 2).	RESULTS
34	42	crystals	evidence	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
73	82	truncated	protein_state	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
117	122	ACBD3	protein	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
123	131	Q domain	structure_element	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
140	157	N-terminal region	structure_element	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
161	166	PI4KB	protein	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
32	52	isotopically labeled	protein_state	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
53	58	ACBD3	protein	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
59	67	Q domain	structure_element	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
72	92	isotopically labeled	protein_state	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
93	98	ACBD3	protein	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
99	107	Q domain	structure_element	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
108	113	PI4KB	protein	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
114	131	N-terminal region	structure_element	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
157	173	NMR spectroscopy	experimental_method	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
7	24	N-terminal region	structure_element	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
57	70	co-expression	experimental_method	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
152	155	15N	chemical	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
156	159	13C	chemical	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
160	168	labelled	protein_state	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
68	72	free	protein_state	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
73	78	ACBD3	protein	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
79	87	Q domain	structure_element	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
127	141	2D 15N/1H HSQC	experimental_method	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
142	149	spectra	evidence	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
215	243	triple-resonance experiments	experimental_method	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
24	27	15N	chemical	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
32	34	1H	chemical	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
44	48	free	protein_state	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
49	54	ACBD3	protein	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
55	63	Q domain	structure_element	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
143	152	Met1-Lys4	residue_range	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
158	163	Gln44	residue_name_number	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
70	74	free	protein_state	Over 93% of non-exchangeable side-chain signals were assigned for the free ACBD3 Q domain.	RESULTS
75	80	ACBD3	protein	Over 93% of non-exchangeable side-chain signals were assigned for the free ACBD3 Q domain.	RESULTS
81	89	Q domain	structure_element	Over 93% of non-exchangeable side-chain signals were assigned for the free ACBD3 Q domain.	RESULTS
85	88	Gln	residue_name	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
96	99	Gln	residue_name	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
112	117	Gln44	residue_name_number	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
133	138	Gln48	residue_name_number	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
234	243	glutamine	residue_name	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
53	60	spectra	evidence	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
155	158	Gln	residue_name	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
160	165	ACBD3	protein	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
171	175	Ala2	residue_name_number	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
177	182	PI4KB	protein	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
25	28	15N	chemical	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
30	33	13C	chemical	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
38	40	1H	chemical	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
99	103	NOEs	evidence	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
122	142	3D 15N/1H NOESY-HSQC	experimental_method	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
147	164	13C/1H HMQC-NOESY	experimental_method	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
165	172	spectra	evidence	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
204	226	structural calculation	experimental_method	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
0	21	Structural statistics	evidence	Structural statistics for the final water-refined sets of structures are shown in SI Table 1.	RESULTS
58	68	structures	evidence	Structural statistics for the final water-refined sets of structures are shown in SI Table 1.	RESULTS
5	14	structure	evidence	This structure revealed that the Q domain forms a two helix hairpin.	RESULTS
33	41	Q domain	structure_element	This structure revealed that the Q domain forms a two helix hairpin.	RESULTS
50	67	two helix hairpin	structure_element	This structure revealed that the Q domain forms a two helix hairpin.	RESULTS
10	15	helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
46	51	helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
84	102	three helix bundle	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
133	138	helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
146	151	PI4KB	protein	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
173	178	44–64	residue_range	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
218	230	kinase helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
14	26	kinase helix	structure_element	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
55	60	Val42	residue_name_number	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
62	67	Ile43	residue_name_number	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
73	78	Asp44	residue_name_number	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
26	31	PI4KB	protein	The remaining part of the PI4KB N-termini, however, is disordered (SI Fig. 5).	RESULTS
18	29	PI4KB:ACBD3	complex_assembly	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
30	58	interactions are hydrophobic	bond_interaction	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
81	95	hydrogen bonds	bond_interaction	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
123	128	ACBD3	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
129	135	Tyr261	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
140	145	PI4KB	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
146	151	His63	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
182	187	ACBD3	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
188	194	Tyr288	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
203	208	PI4KB	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
219	224	Asp44	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
33	38	PI4KB	protein	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
39	44	helix	structure_element	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
48	59	amphipathic	protein_state	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
68	87	hydrophobic surface	site	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
101	109	Q domain	structure_element	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
19	34	structural data	evidence	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
39	49	introduced	experimental_method	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
62	77	point mutations	experimental_method	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
135	159	in vitro pull-down assay	experimental_method	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
0	9	Wild type	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
10	15	ACBD3	protein	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
24	35	co-purified	experimental_method	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
72	83	His6-tagged	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
84	93	wild type	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
94	99	PI4KB	protein	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
120	125	PI4KB	protein	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
126	130	V42A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
135	139	V47A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
140	147	mutants	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
162	169	mutants	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
190	207	binding interface	site	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
209	213	I43A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
215	219	V55A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
221	225	L56A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
14	23	wild type	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
24	29	PI4KB	protein	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
50	55	ACBD3	protein	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
56	61	Y266A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
62	68	mutant	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
91	96	Y285A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
97	103	mutant	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
122	127	F258A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
129	134	H284A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
140	145	Y288A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
146	153	mutants	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
0	5	ACBD3	protein	ACBD3 efficiently recruits the PI4KB enzyme to membranes	RESULTS
31	36	PI4KB	protein	ACBD3 efficiently recruits the PI4KB enzyme to membranes	RESULTS
35	46	ACBD3:PI4KB	complex_assembly	We next sought to determine if the ACBD3:PI4KB interaction drives membrane localization of the PI4KB enzyme.	RESULTS
95	100	PI4KB	protein	We next sought to determine if the ACBD3:PI4KB interaction drives membrane localization of the PI4KB enzyme.	RESULTS
36	72	in vitro membrane recruitment system	experimental_method	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
79	105	Giant Unilamellar Vesicles	experimental_method	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
107	111	GUVs	experimental_method	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
128	133	PI4KB	protein	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
150	152	PI	chemical	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
17	22	PI4KB	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
23	29	kinase	protein_type	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
47	56	localized	evidence	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
75	79	GUVs	experimental_method	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
139	144	ACBD3	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
167	171	GUVs	experimental_method	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
195	200	ACBD3	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
209	227	DGS-NTA (Ni) lipid	chemical	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
246	251	PI4KB	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
24	29	ACBD3	protein	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
55	75	localization signals	evidence	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
80	85	PI4KB	protein	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
87	101	overexpression	experimental_method	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
109	117	Q domain	structure_element	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
163	169	kinase	protein_type	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
224	229	PI4KB	protein	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
259	273	overexpressing	experimental_method	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
278	281	GFP	experimental_method	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
284	292	Q domain	structure_element	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
25	31	signal	evidence	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
67	73	kinase	protein_type	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
179	185	signal	evidence	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
194	208	overexpression	experimental_method	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
212	215	GFP	experimental_method	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
227	238	non-binding	protein_state	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
239	247	Q domain	structure_element	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
248	254	mutant	protein_state	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
276	288	localization	evidence	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
307	312	PI4KB	protein	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
19	33	overexpression	experimental_method	Given this result, overexpression of the Q domain should also interfere with the PI4KB dependent Golgi functions.	RESULTS
41	49	Q domain	structure_element	Given this result, overexpression of the Q domain should also interfere with the PI4KB dependent Golgi functions.	RESULTS
81	86	PI4KB	protein	Given this result, overexpression of the Q domain should also interfere with the PI4KB dependent Golgi functions.	RESULTS
0	8	Ceramide	chemical	Ceramide transport and accumulation in Golgi is a well-known PI4KB dependent process.	RESULTS
61	66	PI4KB	protein	Ceramide transport and accumulation in Golgi is a well-known PI4KB dependent process.	RESULTS
13	34	fluorescently labeled	protein_state	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
35	43	ceramide	chemical	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
107	121	overexpressing	experimental_method	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
126	134	Q domain	structure_element	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
39	47	ceramide	chemical	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
74	84	expressing	experimental_method	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
89	91	wt	protein_state	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
92	100	Q domain	structure_element	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
124	127	RFP	experimental_method	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
135	141	mutant	protein_state	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
142	150	Q domain	structure_element	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
163	171	ceramide	chemical	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
207	218	ACBD3:PI4KB	complex_assembly	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
36	47	ACBD3:PI4KB	complex_assembly	We further analyzed the function of ACBD3:PI4KB interaction in membrane recruitment of PI4KB in living cells using fluorescently tagged proteins.	RESULTS
87	92	PI4KB	protein	We further analyzed the function of ACBD3:PI4KB interaction in membrane recruitment of PI4KB in living cells using fluorescently tagged proteins.	RESULTS
115	135	fluorescently tagged	protein_state	We further analyzed the function of ACBD3:PI4KB interaction in membrane recruitment of PI4KB in living cells using fluorescently tagged proteins.	RESULTS
12	21	rapamycin	chemical	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
52	58	FKBP12	protein	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
60	84	FK506 binding protein 12	protein	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
90	93	FRB	structure_element	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
95	103	fragment	structure_element	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
107	111	mTOR	protein	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
123	132	rapamycin	chemical	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
3	8	fused	experimental_method	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
13	16	FRB	structure_element	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
29	34	34–63	residue_range	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
42	75	mitochondrial localization signal	structure_element	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
81	120	mitochondrial A-kinase anchor protein 1	protein	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
122	127	AKAP1	protein	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
133	136	CFP	experimental_method	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
4	9	ACBD3	protein	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
10	18	Q domain	structure_element	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
28	36	fused to	experimental_method	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
37	43	FKBP12	protein	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
48	52	mRFP	experimental_method	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
12	24	localization	evidence	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
32	37	ACBD3	protein	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
38	46	Q domain	structure_element	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
51	54	GFP	experimental_method	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
57	62	PI4KB	protein	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
96	105	rapamycin	chemical	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
21	26	H284A	mutant	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
27	33	mutant	protein_state	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
41	46	ACBD3	protein	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
47	55	Q domain	structure_element	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
89	94	PI4KB	protein	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
95	101	kinase	protein_type	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
18	23	ACDB3	protein	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
24	32	Q domain	structure_element	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
121	130	rapamycin	chemical	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
145	154	wild-type	protein_state	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
188	194	kinase	protein_type	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
35	38	GFP	experimental_method	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
39	44	PI4KB	protein	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
45	51	kinase	protein_type	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
55	67	co-expressed	experimental_method	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
77	86	wild-type	protein_state	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
87	92	ACDB3	protein	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
93	101	Q domain	structure_element	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
129	141	localization	evidence	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
9	14	PI4KB	protein	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
32	44	localization	evidence	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
50	62	co-expressed	experimental_method	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
72	87	non-interacting	protein_state	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
88	96	Q domain	structure_element	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
97	103	mutant	protein_state	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
0	5	ACBD3	protein	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
16	21	PI4KB	protein	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
22	40	enzymatic activity	evidence	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
55	60	PI4KB	protein	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
16	21	ACBD3	protein	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
36	41	PI4KB	protein	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
42	48	kinase	protein_type	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
49	67	enzymatic activity	evidence	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
92	116	luminescent kinase assay	experimental_method	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
123	125	PI	chemical	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
29	35	kinase	protein_type	We observed no effect on the kinase activity of PI4KB (Fig. 4A) suggesting that ACBD3 does not directly affect the enzyme (e.g. induction of a conformation change).	RESULTS
48	53	PI4KB	protein	We observed no effect on the kinase activity of PI4KB (Fig. 4A) suggesting that ACBD3 does not directly affect the enzyme (e.g. induction of a conformation change).	RESULTS
80	85	ACBD3	protein	We observed no effect on the kinase activity of PI4KB (Fig. 4A) suggesting that ACBD3 does not directly affect the enzyme (e.g. induction of a conformation change).	RESULTS
17	22	ACBD3	protein	However, in vivo ACBD3 is located at the Golgi membranes, whereas in this experiment, ACBD3 was located in the solution and PI is provided as micelles.	RESULTS
86	91	ACBD3	protein	However, in vivo ACBD3 is located at the Golgi membranes, whereas in this experiment, ACBD3 was located in the solution and PI is provided as micelles.	RESULTS
124	126	PI	chemical	However, in vivo ACBD3 is located at the Golgi membranes, whereas in this experiment, ACBD3 was located in the solution and PI is provided as micelles.	RESULTS
33	36	GUV	experimental_method	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
49	54	ACBD3	protein	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
55	64	localized	evidence	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
72	75	GUV	experimental_method	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
4	8	GUVs	experimental_method	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
23	25	PI	chemical	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
54	59	PI4KB	protein	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
60	66	kinase	protein_type	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
26	29	CFP	experimental_method	The buffer also contained CFP-SidC, which binds to PI4P with nanomolar affinity.	RESULTS
30	34	SidC	protein	The buffer also contained CFP-SidC, which binds to PI4P with nanomolar affinity.	RESULTS
51	55	PI4P	chemical	The buffer also contained CFP-SidC, which binds to PI4P with nanomolar affinity.	RESULTS
34	40	kinase	protein_type	This enabled visualization of the kinase reaction using a confocal microscope.	RESULTS
58	77	confocal microscope	experimental_method	This enabled visualization of the kinase reaction using a confocal microscope.	RESULTS
34	49	phosphorylation	ptm	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
66	72	kinase	protein_type	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
73	78	alone	protein_state	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
92	98	kinase	protein_type	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
131	135	GUVs	experimental_method	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
139	144	ACBD3	protein	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
35	45	absence of	protein_state	Reaction was also performed in the absence of ATP as a negative control (Fig. 4B).	RESULTS
46	49	ATP	chemical	Reaction was also performed in the absence of ATP as a negative control (Fig. 4B).	RESULTS
30	35	PI4KB	protein	These experiments showed that PI4KB enzymatic activity increases when ACBD3 is membrane localized (Fig. 4C, SI Fig. 6).	RESULTS
36	54	enzymatic activity	evidence	These experiments showed that PI4KB enzymatic activity increases when ACBD3 is membrane localized (Fig. 4C, SI Fig. 6).	RESULTS
70	75	ACBD3	protein	These experiments showed that PI4KB enzymatic activity increases when ACBD3 is membrane localized (Fig. 4C, SI Fig. 6).	RESULTS
24	29	PI4KB	protein	Membrane recruitment of PI4KB enzyme is crucial to ensure its proper function at the Golgi and TGN.	DISCUSS
58	63	PI4KB	protein	However, the molecular mechanism and structural basis for PI4KB interaction with the membrane is poorly understood.	DISCUSS
45	50	PI4KB	protein	In principle, any of the binding partners of PI4KB could play a role in membrane recruitment.	DISCUSS
17	22	PI4KB	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
78	91	small GTPases	protein_type	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
92	97	Rab11	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
102	106	Arf1	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
127	163	acyl-CoA binding domain containing 3	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
165	170	ACBD3	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
181	206	neuronal calcium sensor-1	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
208	213	NCS-1	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
228	237	frequenin	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
241	246	yeast	taxonomy_domain	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
256	271	14-3-3 proteins	protein_type	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
4	13	monomeric	oligomeric_state	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
14	23	G protein	protein_type	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
24	29	Rab11	protein	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
36	45	mammalian	taxonomy_domain	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
46	51	PI4KB	protein	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
64	78	helical domain	structure_element	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
86	92	kinase	protein_type	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
9	14	Rab11	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
65	70	PI4KB	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
85	90	PI4KB	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
128	133	Rab11	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
0	4	Arf1	protein	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
16	41	small GTP binding protein	protein_type	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
98	103	PI4KB	protein	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
154	159	PI4KB	protein	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
4	9	yeast	taxonomy_domain	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
23	27	NCS1	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
35	44	frequenin	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
77	82	Pik1p	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
88	93	yeast	taxonomy_domain	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
108	113	PI4KB	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
194	199	NCS-1	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
203	208	PI4KB	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
224	233	mammalian	taxonomy_domain	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
0	5	NCS-1	protein	NCS-1 is an N-terminally myristoylated protein that participates in exocytosis.	DISCUSS
25	38	myristoylated	protein_state	NCS-1 is an N-terminally myristoylated protein that participates in exocytosis.	DISCUSS
81	86	PI4KB	protein	It is expressed only in certain cell types, suggesting that if it contributes to PI4KB membrane recruitment, it does so in a tissues specific manner.	DISCUSS
19	24	PI4KB	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
30	45	14-3-3 proteins	protein_type	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
59	74	phosphorylation	ptm	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
78	83	PI4KB	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
87	103	protein kinase D	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
132	137	PI4KB	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
157	163	active	protein_state	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
9	24	14-3-3 proteins	protein_type	However, 14-3-3 proteins do not appear to interfere with membrane recruitment of this kinase.	DISCUSS
86	92	kinase	protein_type	However, 14-3-3 proteins do not appear to interfere with membrane recruitment of this kinase.	DISCUSS
0	5	ACBD3	protein	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
35	44	conserved	protein_state	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
51	62	vertebrates	taxonomy_domain	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
105	110	PI4KB	protein	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
228	234	kinase	protein_type	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
55	60	PI4KB	protein	For these reasons we focused on the interaction of the PI4KB enzyme with the Golgi resident ACBD3 protein in this study.	DISCUSS
92	97	ACBD3	protein	For these reasons we focused on the interaction of the PI4KB enzyme with the Golgi resident ACBD3 protein in this study.	DISCUSS
58	63	PI4KB	protein	Here we present the mechanism for membrane recruitment of PI4KB by the Golgi resident ACBD3 protein.	DISCUSS
86	91	ACBD3	protein	Here we present the mechanism for membrane recruitment of PI4KB by the Golgi resident ACBD3 protein.	DISCUSS
53	55	Kd	evidence	We show that these proteins interact directly with a Kd value in the submicromolar range.	DISCUSS
41	46	PI4KB	protein	The interaction is sufficient to recruit PI4KB to model membranes in vitro as well as to the mitochondria where PI4KB is never naturally found.	DISCUSS
112	117	PI4KB	protein	The interaction is sufficient to recruit PI4KB to model membranes in vitro as well as to the mitochondria where PI4KB is never naturally found.	DISCUSS
50	56	solved	experimental_method	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
61	79	solution structure	evidence	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
83	94	ACBD3:PI4KB	complex_assembly	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
136	141	PI4KB	protein	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
142	159	N-terminal region	structure_element	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
171	193	short amphipatic helix	structure_element	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
204	209	44–64	residue_range	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
226	231	ACBD3	protein	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
232	240	Q domain	structure_element	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
4	12	Q domain	structure_element	The Q domain adopts a helical hairpin fold that is further stabilized upon binding the kinase helix (Fig. 2A).	DISCUSS
22	42	helical hairpin fold	structure_element	The Q domain adopts a helical hairpin fold that is further stabilized upon binding the kinase helix (Fig. 2A).	DISCUSS
87	99	kinase helix	structure_element	The Q domain adopts a helical hairpin fold that is further stabilized upon binding the kinase helix (Fig. 2A).	DISCUSS
115	121	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
173	178	ACBD3	protein	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
214	220	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
271	277	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
377	383	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
38	48	structures	evidence	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
60	78	pseudoatomic model	evidence	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
82	87	PI4KB	protein	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
254	259	Rab11	protein	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
0	12	+RNA viruses	taxonomy_domain	+RNA viruses replicate at specific PI4P-enriched membranous compartments.	DISCUSS
35	39	PI4P	chemical	+RNA viruses replicate at specific PI4P-enriched membranous compartments.	DISCUSS
61	66	viral	taxonomy_domain	These are called replication factories (because they enhance viral replication) or membranous webs (because of their appearance under the electron microscope).	DISCUSS
35	42	viruses	taxonomy_domain	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
85	89	PI4K	protein_type	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
90	97	kinases	protein_type	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
128	132	PI4P	chemical	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
133	138	lipid	chemical	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
0	26	Non-structural 3A proteins	protein_type	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
37	51	picornaviruses	taxonomy_domain	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
61	72	Enterovirus	taxonomy_domain	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
79	89	poliovirus	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
91	108	coxsackievirus-B3	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
110	123	rhinovirus-14	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
129	138	Kobuvirus	taxonomy_domain	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
145	158	Aichi virus-1	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
190	195	ACBD3	protein	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
45	59	3A:ACBD3:PI4KB	complex_assembly	Our data suggest that they could do this via 3A:ACBD3:PI4KB complex formation.	DISCUSS
4	13	structure	evidence	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
21	26	ACBD3	protein	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
27	35	Q domain	structure_element	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
44	56	kinase helix	structure_element	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
137	142	ACBD3	protein	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
144	149	PI4KB	protein	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
159	170	ACBD3:PI4KB	complex_assembly	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
186	198	picornaviral	taxonomy_domain	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
79	93	picornaviruses	taxonomy_domain	This could eventually have implications for therapeutic intervention to combat picornaviruses-mediated diseases ranging from polio to the common cold.	DISCUSS
0	28	Biochemical characterization	experimental_method	Biochemical characterization of the ACBD3:PI4KB complex.	FIG
36	47	ACBD3:PI4KB	complex_assembly	Biochemical characterization of the ACBD3:PI4KB complex.	FIG
36	41	ACBD3	protein	(A) Schematic representation of the ACBD3 and PI4KB constructs used for the experiments.	FIG
46	51	PI4KB	protein	(A) Schematic representation of the ACBD3 and PI4KB constructs used for the experiments.	FIG
0	5	ACBD3	protein	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
19	42	acyl-CoA binding domain	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
44	48	ACBD	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
51	77	charged amino acids region	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
79	82	CAR	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
85	106	glutamine rich region	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
108	109	Q	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
116	137	Golgi dynamics domain	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
139	143	GOLD	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
0	5	PI4KB	protein	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
25	42	N-terminal region	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
44	58	helical domain	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
64	77	kinase domain	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
104	127	N- and C-terminal lobes	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
4	28	In vitro pull-down assay	experimental_method	(B) In vitro pull-down assay.	FIG
0	16	Pull-down assays	experimental_method	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
67	81	His6GB1-tagged	protein_state	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
108	116	untagged	protein_state	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
117	128	full-length	protein_state	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
129	134	PI4KB	protein	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
138	143	ACBD3	protein	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
47	55	SDS gels	experimental_method	The inputs and bound proteins were analyzed on SDS gels stained with Coomassie Blue.	FIG
35	46	full-length	protein_state	Please, see SI Fig. 9 for original full-length gels. (C) Analytical Ultracentrifugation.	FIG
57	87	Analytical Ultracentrifugation	experimental_method	Please, see SI Fig. 9 for original full-length gels. (C) Analytical Ultracentrifugation.	FIG
0	3	AUC	experimental_method	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
20	31	ACBD3:PI4KB	complex_assembly	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
32	43	full-length	protein_state	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
113	152	ACBD3 Q domain: PI4KB N terminal region	complex_assembly	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
225	250	Surface plasmon resonance	experimental_method	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
0	3	SPR	experimental_method	SPR analysis of the PI4KB binding to immobilized ACBD3.	FIG
20	25	PI4KB	protein	SPR analysis of the PI4KB binding to immobilized ACBD3.	FIG
49	54	ACBD3	protein	SPR analysis of the PI4KB binding to immobilized ACBD3.	FIG
0	11	Sensorgrams	evidence	Sensorgrams for four concentrations of PI4KB are shown.	FIG
39	44	PI4KB	protein	Sensorgrams for four concentrations of PI4KB are shown.	FIG
0	19	Structural analysis	experimental_method	Structural analysis of the ACBD3:PI4KB complex.	FIG
27	38	ACBD3:PI4KB	complex_assembly	Structural analysis of the ACBD3:PI4KB complex.	FIG
12	21	structure	evidence	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
29	34	ACBD3	protein	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
35	43	Q domain	structure_element	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
58	73	in complex with	protein_state	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
78	83	PI4KB	protein	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
84	101	N-terminal region	structure_element	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
0	13	Superposition	experimental_method	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
34	44	structures	evidence	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
62	70	Q domain	structure_element	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
98	108	structures	evidence	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
158	164	folded	protein_state	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
173	178	PI4KB	protein	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
43	57	hydrogen bonds	bond_interaction	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
59	64	ACBD3	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
65	71	Tyr261	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
73	78	PI4KB	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
79	84	His63	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
89	94	ACBD3	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
95	101	Tyr288	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
103	108	PI4KB	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
109	114	Asp44	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
127	146	hydrophobic surface	site	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
154	166	kinase helix	structure_element	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
180	185	ACBD3	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
186	194	Q domain	structure_element	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
0	5	ACBD3	protein	ACBD3 is shown in magenta and PI4KB in orange.	FIG
30	35	PI4KB	protein	ACBD3 is shown in magenta and PI4KB in orange.	FIG
20	32	kinase helix	structure_element	(C) Top view of the kinase helix.	FIG
4	16	kinase helix	structure_element	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
20	31	amphipathic	protein_state	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
40	59	hydrophobic surface	site	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
78	83	ACBD3	protein	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
84	99	binding surface	site	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
160	175	Pull-down assay	experimental_method	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
214	228	His6GB1-tagged	protein_state	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
229	234	PI4KB	protein	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
235	241	kinase	protein_type	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
246	254	untagged	protein_state	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
255	260	ACBD3	protein	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
0	9	Wild type	protein_state	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
38	45	mutants	protein_state	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
54	59	PI4KB	protein	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
64	69	ACBD3	protein	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
35	46	full-length	protein_state	Please, see SI Fig. 9 for original full-length gels.	FIG
0	5	ACBD3	protein	ACBD3 is sufficient to recruit the PI4KB kinase to membranes.	FIG
35	40	PI4KB	protein	ACBD3 is sufficient to recruit the PI4KB kinase to membranes.	FIG
41	47	kinase	protein_type	ACBD3 is sufficient to recruit the PI4KB kinase to membranes.	FIG
4	26	GUVs recruitment assay	experimental_method	(A) GUVs recruitment assay.	FIG
34	40	kinase	protein_type	Top – Virtually no membrane bound kinase was observed when 600 nM PI4KB was added to the GUVs.	FIG
66	71	PI4KB	protein	Top – Virtually no membrane bound kinase was observed when 600 nM PI4KB was added to the GUVs.	FIG
89	93	GUVs	experimental_method	Top – Virtually no membrane bound kinase was observed when 600 nM PI4KB was added to the GUVs.	FIG
16	27	presence of	protein_state	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
35	47	GUV tethered	protein_state	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
48	53	ACBD3	protein	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
82	88	kinase	protein_type	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
119	123	GUVs	experimental_method	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
4	33	Golgi displacement experiment	experimental_method	(B) Golgi displacement experiment.	FIG
13	18	ACBD3	protein	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
19	27	Q domain	structure_element	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
37	40	GFP	experimental_method	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
45	58	overexpressed	experimental_method	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
78	83	PI4KB	protein	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
88	101	immunostained	experimental_method	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
49	52	GFP	experimental_method	Middle panel: The same experiment performed with GFP alone.	FIG
48	54	mutant	protein_state	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
55	63	Q domain	structure_element	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
65	70	F258A	mutant	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
72	77	H284A	mutant	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
79	84	Y288A	mutant	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
109	114	PI4KB	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
120	125	ACBD3	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
126	134	Q domain	structure_element	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
135	149	overexpression	experimental_method	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
159	167	ceramide	chemical	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
218	227	wild-type	protein_state	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
228	233	ACBD3	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
234	242	Q domain	structure_element	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
243	247	FKBP	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
248	252	mRFP	experimental_method	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
278	296	Bodipy FL-Ceramide	chemical	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
50	54	mRFP	experimental_method	Middle panel – The same experiment performed with mRFP-FKBP alone.	FIG
55	59	FKBP	protein	Middle panel – The same experiment performed with mRFP-FKBP alone.	FIG
49	55	mutant	protein_state	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
56	64	Q domain	structure_element	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
66	71	F258A	mutant	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
73	78	H284A	mutant	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
80	85	Y288A	mutant	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
110	115	PI4KB	protein	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
135	170	mitochondria recruitment experiment	experimental_method	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
6	11	AKAP1	protein	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
12	15	FRB	structure_element	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
16	19	CFP	experimental_method	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
33	42	localized	evidence	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
90	93	GFP	experimental_method	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
94	99	PI4KB	protein	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
104	112	Q domain	structure_element	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
113	117	FKBP	protein	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
118	122	mRFP	experimental_method	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
138	147	localized	evidence	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
17	26	rapamycin	chemical	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
31	39	Q domain	structure_element	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
40	44	FKBP	protein	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
45	49	mRFP	experimental_method	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
103	106	GFP	experimental_method	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
107	112	PI4KB	protein	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
126	161	Mitochondria recruitment experiment	experimental_method	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
30	35	AKAP1	protein	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
36	39	FRB	structure_element	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
40	43	CFP	experimental_method	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
45	48	GFP	experimental_method	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
49	54	PI4KB	protein	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
59	68	wild-type	protein_state	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
69	77	Q domain	structure_element	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
78	82	FKBP	protein	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
83	87	mRFP	experimental_method	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
141	150	rapamycin	chemical	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
48	53	H264A	mutant	Right – The same experiment performed using the H264A Q domain mutant.	FIG
54	62	Q domain	structure_element	Right – The same experiment performed using the H264A Q domain mutant.	FIG
63	69	mutant	protein_state	Right – The same experiment performed using the H264A Q domain mutant.	FIG
0	5	ACBD3	protein	ACBD3 indirectly increases the activity of PI4KB.	FIG
43	48	PI4KB	protein	ACBD3 indirectly increases the activity of PI4KB.	FIG
4	31	Micelles-based kinase assay	experimental_method	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
34	36	PI	chemical	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
69	93	luminescent kinase assay	experimental_method	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
116	120	PI4P	chemical	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
38	42	PI4P	chemical	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
60	71	presence of	protein_state	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
127	131	PI4P	chemical	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
145	150	PI4KB	protein	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
15	42	standard errors of the mean	evidence	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
44	47	SEM	evidence	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
93	124	GUV-based phosphorylation assay	experimental_method	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
127	131	GUVs	experimental_method	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
147	149	PI	chemical	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
197	201	PI4P	chemical	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
225	243	CFP-SidC biosensor	experimental_method	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
26	51	GUV phosphorylation assay	experimental_method	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
54	90	Mean membrane fluorescence intensity	evidence	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
98	102	PI4P	chemical	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
113	117	SidC	protein	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
149	152	ATP	chemical	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
4	27	mean membrane intensity	evidence	The mean membrane intensity value is relative to the background signal and the difference between the membrane and background signal in the reference system lacking ATP.	FIG
165	168	ATP	chemical	The mean membrane intensity value is relative to the background signal and the difference between the membrane and background signal in the reference system lacking ATP.	FIG
25	28	SEM	evidence	The error bars stand for SEM based on three independent experiments (also SI Fig. 6).	FIG
0	18	Pseudoatomic model	evidence	Pseudoatomic model of the PI4KB multiprotein complex assembly.	FIG
26	31	PI4KB	protein	Pseudoatomic model of the PI4KB multiprotein complex assembly.	FIG
0	5	PI4KB	protein	PI4KB in orange, Rab11 in purple, ACBD3 in blue.	FIG
17	22	Rab11	protein	PI4KB in orange, Rab11 in purple, ACBD3 in blue.	FIG
34	39	ACBD3	protein	PI4KB in orange, Rab11 in purple, ACBD3 in blue.	FIG
26	29	NMR	experimental_method	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
30	39	structure	evidence	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
67	84	crystal structure	evidence	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
88	99	PI4KB:Rab11	complex_assembly	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
125	129	ACBD	structure_element	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
134	138	GOLD	structure_element	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
151	167	homology modeled	experimental_method	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
200	210	structures	evidence	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
227	233	Phyre2	experimental_method	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
4	8	GOLD	structure_element	The GOLD domain is tethered to the membrane by GolginB1 (also known as Giantin) which is not shown for clarity.	FIG
47	55	GolginB1	protein	The GOLD domain is tethered to the membrane by GolginB1 (also known as Giantin) which is not shown for clarity.	FIG
71	78	Giantin	protein	The GOLD domain is tethered to the membrane by GolginB1 (also known as Giantin) which is not shown for clarity.	FIG
0	32	Intrinsically disordered linkers	structure_element	Intrinsically disordered linkers are modeled in an arbitrary but physically plausible conformation.	FIG