The impact of IDR phosphorylation on the RNA binding profiles of proteins

Many intrinsically disordered regions (IDRs) can be phosphorylated.Phosphorylation of IDRs can change their conformation and functions.Structural rearrangements of IDRs can influence the interaction of proteins with RNA.IDR phosphorylation can selectively alter global 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 (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. 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.