LMP7 inhibits the activation of NLRP3 inflammasome through interaction with NLRP3.
The innate immune system recognizes pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs) by coding pattern recognition receptors (PRRs). As a well-known inflammasome, NLRP3 plays an essential role in helping the host immune response and driving antiviral processes. Low molecular mass polypeptide (LMP7) is a critical component of the immunoproteasome that participates in host antiviral activity, as well as T cell function and development. This is the first study to report the direct interaction between LMP7 and NLRP3. Also, LMP7 was found to inhibit the activation of the NLRP3 inflammasome, which is of great significance in exploring the role of the immune proteasome in regulating the activation of NLRP3.
['Jin|Jing|J|', 'Wang|Wenbiao|W|', 'Li|Aixin|A|', 'Wu|Jianguo|J|']
D002460:Cell Line D003593:Cytoplasm D006801:Humans D058847:Inflammasomes D000071199:NLR Family, Pyrin Domain-Containing 3 Protein D046988:Proteasome Endopeptidase Complex D011485:Protein Binding D000072417:Protein Domains D020798:Two-Hybrid System Techniques
Immune proteasome Low molecular mass polypeptide LMP7 NACHT LRR and PYD domains-Containing protein 3 NLRP3