Arginine methylation an emerging regulator of protein function

Mol Cell. 2005 Apr 29;18(3):263-72. doi: 10.1016/j.molcel.2005.04.003.

Abstract

Arginine methylation is now coming out of the shadows of protein phosphorylation and entering the mainstream, largely due to the identification of the family of enzymes that lay down this modification. In addition, modification-specific antibodies and proteomic approaches have facilitated the identification of an array of substrates for the protein arginine methyltransferases. This review describes recent insights into the molecular processes regulated by arginine methylation in normal and diseased cells.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Oxidoreductases / metabolism
  • Animals
  • Arginine / chemistry
  • Arginine / metabolism*
  • Disease
  • Humans
  • Methylation
  • Molecular Structure
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism*
  • RNA Processing, Post-Transcriptional
  • Signal Transduction / physiology

Substances

  • Arginine
  • Amino Acid Oxidoreductases
  • Protein-Arginine N-Methyltransferases