%0 Journal Article
%T The impact of IDR phosphorylation on the RNA binding profiles of proteins.
%A Modic M
%A Adamek M
%A Ule J
%J Trends Genet
%V 40
%N 7
%D 2024 Jul 4
%M 38705823
%F 11.821
%R 10.1016/j.tig.2024.04.004
%X 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 (PTMs). 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.