Protein interfaces in signaling regulated by arginine methylation

Sci STKE. 2005 Feb 15;2005(271):re2. doi: 10.1126/stke.2712005re2.

Abstract

Posttranslational modifications are well-known effectors of signal transduction. Arginine methylation is a covalent modification that results in the addition of methyl groups to the nitrogen atoms of the arginine side chains. A probable role of arginine methylation in signal transduction is emerging with the identification of new arginine-methylated proteins. However, the functional consequences of arginine methylation and its mode of regulation remain unknown. The identification of the protein arginine methyltransferase family and the development of methylarginine-specific antibodies have raised renewed interest in this modification during the last decade. 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 signaling by interferon and cytokines, and in T cell signaling. We discuss these recent advances and the role of arginine methylation in signal transduction.

Publication types

  • Review

MeSH terms

  • Animals
  • Arginine / chemistry*
  • Consensus Sequence
  • Drosophila Proteins / physiology
  • Eukaryotic Cells / metabolism
  • Humans
  • Hydrogen Bonding
  • Hydrolases / metabolism
  • Hydrophobic and Hydrophilic Interactions
  • Methylation
  • NFATC Transcription Factors / metabolism
  • Phylogeny
  • Plant Proteins / physiology
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Processing, Post-Translational*
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases
  • Protein-Arginine N-Methyltransferases / classification
  • Protein-Arginine N-Methyltransferases / physiology*
  • Saccharomyces cerevisiae Proteins / physiology
  • Signal Transduction / physiology*
  • Substrate Specificity

Substances

  • Drosophila Proteins
  • NFATC Transcription Factors
  • Plant Proteins
  • Saccharomyces cerevisiae Proteins
  • Arginine
  • Protein-Arginine N-Methyltransferases
  • Hydrolases
  • PADI4 protein, human
  • Protein-Arginine Deiminase Type 4
  • Protein-Arginine Deiminases