The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation

Thomas B. Nicholson, Taiping Chen, Stéphane Richard

Research output: Contribution to journalReview articlepeer-review

112 Scopus citations

Abstract

Post-translational modifications are well-known effectors in DNA damage signaling and epigenetic gene expression. Protein arginine methylation is a covalent modification that results in the addition of methyl groups to the nitrogen atoms of the arginine side chains and is catalyzed by a family of protein arginine methyltransferases (PRMTs). In the past, arginine methylation was mainly observed on abundant proteins such as RNA-binding proteins and histones, but recent advances have revealed a plethora of arginine-methylated proteins implicated in a variety of cellular processes including signal transduction, epigenetic regulation and DNA repair pathways. Herein, we discuss these recent advances, focusing on the role of PRMT1, the major asymmetric arginine methyltransferase, in cellular processes and its link to human diseases.

Original languageEnglish (US)
Pages (from-to)466-474
Number of pages9
JournalPharmacological Research
Volume60
Issue number6
DOIs
StatePublished - Dec 2009
Externally publishedYes

Keywords

  • Arginine methylation
  • DNA damage
  • Disease
  • PRMT1
  • Post-translational modifications

ASJC Scopus subject areas

  • Pharmacology

Fingerprint

Dive into the research topics of 'The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation'. Together they form a unique fingerprint.

Cite this