Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila.
The Paip2 protein is a factor regulating mRNA translation and stability in the cytoplasm. It has also been found in the nuclei of several cell types in Drosophila. Here, we aim to elucidate the functions of Paip2 in the cell nucleus. We find that nuclear Paip2 is a component of an ~300-kDa protein complex. Paip2 interacts with mRNA capping factor and factors of RNA polymerase II (Pol II) transcription initiation and early elongation. Paip2 functionally cooperates with the Cbp80 subunit of the cap-binding complex, with both proteins ensuring proper Pol II C-terminal domain (CTD) Ser5 phosphorylation at the promoter. Thus, Paip2 is a novel player at the stage of mRNA capping and early Pol II elongation.
['Kachaev|Zaur M|ZM|', 'Lebedeva|Lyubov A|LA|', 'Shaposhnikov|Alexander V|AV|', 'Moresco|James J|JJ|', 'Yates|John R|JR|', 'Schedl|Paul|P|', 'Shidlovskii|Yulii V|YV|0000-0002-3643-9889']
D000818:Animals D002460:Cell Line D004247:DNA D029721:Drosophila Proteins D004331:Drosophila melanogaster D005786:Gene Expression Regulation D039502:Nuclear Cap-Binding Protein Complex D010766:Phosphorylation D039102:Poly(A)-Binding Proteins D011401:Promoter Regions, Genetic D011499:Protein Processing, Post-Translational D012319:RNA Polymerase II
Paip2 Cbp80 promoter protein complex capping transcription