{Reference Type}: Journal Article
{Title}: The impact of IDR phosphorylation on the RNA binding profiles of proteins.
{Author}: Modic M;Adamek M;Ule J;
{Journal}: Trends Genet
{Volume}: 40
{Issue}: 7
{Year}: 2024 Jul 4
{Factor}: 11.821
{DOI}: 10.1016/j.tig.2024.04.004
{Abstract}: 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.