Paip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila.

TitlePaip2 cooperates with Cbp80 at an active promoter and participates in RNA Polymerase II phosphorylation in Drosophila.
Publication TypeJournal Article
Year of Publication2019
AuthorsKachaev, ZM, Lebedeva, LA, Shaposhnikov, AV, Moresco, JJ, Yates, JR, Schedl, P, Shidlovskii, YV
JournalFEBS Lett
Volume593
Issue10
Pagination1102-1112
Date Published2019 May
ISSN1873-3468
Abstract

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.

DOI10.1002/1873-3468.13391
Alternate JournalFEBS Lett.
PubMed ID31001806
Grant List8 P41GM103533 / / National Institute of General Medical Sciences /
R35 GM126975 / / National Institute of General Medical Sciences /
16-14-10346 / / Russian Science Foundation /
P41 GM103533 / GM / NIGMS NIH HHS / United States
R35 GM126975 / GM / NIGMS NIH HHS / United States