Phosphorylation of intrinsically disordered regions steers the protein-RNA binding profiles

Due to their capacity to mediate repetitive protein interactions, intrinsically disordered regions (IDRs) are crucial for the formation of various types of protein-RNA complexes. The functions of IDRs are strongly modulated by post-translational modifications. Phosphorylation is the most common and...

Full description

Saved in:
Bibliographic Details
Published in:Trends in genetics 2024-05, Vol.40 (7), p.580-586
Main Authors: Modic, Miha, Adamek, Maksimiljan, Ule, Jernej
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Due to their capacity to mediate repetitive protein interactions, intrinsically disordered regions (IDRs) are crucial for the formation of various types of protein-RNA complexes. The functions of IDRs are strongly modulated by post-translational modifications. Phosphorylation is the most common and well-studied modification of IDRs, which can alter homomeric or heteromeric interactions of proteins, and impact their ability to phase-separate. Moreover, phosphorylation can influence the RNA-binding properties of proteins, and recent studies demonstrated its selective impact on the global profiles of protein-RNA binding and regulation. These findings highlight the need for further integrative approaches to understand how signalling remodels protein-RNA networks in cells.
ISSN:0168-9525
DOI:10.1016/j.tig.2024.04.004