Protein arginine methylation: Cellular functions and methods of analysis

Biochim Biophys Acta. 2006 Dec;1764(12):1890-903. doi: 10.1016/j.bbapap.2006.08.008. Epub 2006 Aug 25.

Abstract

During the last few years, new members of the growing family of protein arginine methyltransferases (PRMTs) have been identified and the role of arginine methylation in manifold cellular processes like signaling, RNA processing, transcription, and subcellular transport has been extensively investigated. In this review, we describe recent methods and findings that have yielded new insights into the cellular functions of arginine-methylated proteins, and we evaluate the currently used procedures for the detection and analysis of arginine methylation.

Publication types

  • Review

MeSH terms

  • Arginine / analogs & derivatives
  • Arginine / immunology
  • Arginine / metabolism*
  • DNA Repair / physiology
  • F-Box Proteins / metabolism
  • Humans
  • Mass Spectrometry / methods
  • Methyltransferases / metabolism
  • Protein Processing, Post-Translational*
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Proteomics / methods
  • RNA Processing, Post-Transcriptional / drug effects
  • S-Adenosylmethionine / metabolism
  • Signal Transduction / physiology
  • Transcription, Genetic / drug effects

Substances

  • F-Box Proteins
  • symmetric dimethylarginine
  • N,N-dimethylarginine
  • S-Adenosylmethionine
  • Arginine
  • Methyltransferases
  • FBXO11 protein, human
  • PRMT7 protein, human
  • Protein-Arginine N-Methyltransferases