Effectors and effects of arginine methylation

Research output: Contribution to journalReview articlepeer-review

3 Scopus citations

Abstract

Arginine methylation is a ubiquitous and relatively stable post-translational modification (PTM) that occurs in three types: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). Methylarginine marks are catalyzed by members of the protein arginine methyltransferases (PRMTs) family of enzymes. Substrates for arginine methylation are found in most cellular compartments, with RNAbinding proteins forming the majority of PRMT targets. Arginine methylation often occurs in intrinsically disordered regions of proteins, which impacts biological processes like protein-protein interactions and phase separation, to modulate gene transcription, mRNA splicing and signal transduction. With regards to protein-protein interactions, the major 'readers' of methylarginine marks are Tudor domain-containing proteins, although additional domain types and unique protein folds have also recently been identified as methylarginine readers. Here, we will assess the current 'state-of-the-art' in the arginine methylation reader field. We will focus on the biological functions of the Tudor domaincontaining methylarginine readers and address other domains and complexes that sense methylarginine marks.

Original languageEnglish (US)
Pages (from-to)725-734
Number of pages10
JournalBiochemical Society Transactions
Volume51
Issue number2
DOIs
StatePublished - Apr 2023

Keywords

  • phase separation
  • PRMTs
  • R-loops
  • Tudor domains

ASJC Scopus subject areas

  • Biochemistry

Fingerprint

Dive into the research topics of 'Effectors and effects of arginine methylation'. Together they form a unique fingerprint.

Cite this