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

Trends Genet. 2024 Jul;40(7):580-586. doi: 10.1016/j.tig.2024.04.004. Epub 2024 May 4.

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.

Keywords: RNA-binding protein (RBP); RNP condensate; intrinsically disordered region (IDR); phosphorylation; post-translational modification (PTM); protein–RNA network; ribonucleoprotein (RNP) assembly.

Publication types

  • Review

MeSH terms

  • Humans
  • Intrinsically Disordered Proteins* / chemistry
  • Intrinsically Disordered Proteins* / genetics
  • Intrinsically Disordered Proteins* / metabolism
  • Phosphorylation
  • Protein Binding*
  • Protein Processing, Post-Translational* / genetics
  • RNA* / genetics
  • RNA* / metabolism
  • RNA-Binding Proteins* / genetics
  • RNA-Binding Proteins* / metabolism

Substances

  • RNA-Binding Proteins
  • RNA
  • Intrinsically Disordered Proteins