Regulation of histone arginine methylation/demethylation by methylase and demethylase (Review)

Mol Med Rep. 2019 May;19(5):3963-3971. doi: 10.3892/mmr.2019.10111. Epub 2019 Apr 1.

Abstract

Histone arginine methylation is a universal post‑translational modification that has been implicated in multiple cellular and sub‑cellular processes, including pre‑mRNA splicing, DNA damage signaling, mRNA translation, cell signaling and cell death. Despite these important roles, the understanding of its regulation with respect to certain other modifications, such as phosphorylation and acetylation, is very poor. Thus far, few histone arginine demethylases have been identified in mammalian cells, compared with nine protein arginine methyltransferases (PRMTs) that have been reported. Studies have reported that aberrant histone arginine methylation is strongly associated with carcinogenesis and metastasis. This increases the requirement for understanding the regulation of histone arginine demethylation. The present review summarizes the published studies and provides further insights into histone arginine methylases and demethylases.

Publication types

  • Review

MeSH terms

  • DNA Damage
  • Histone Demethylases / chemistry
  • Histone Demethylases / metabolism*
  • Histones / metabolism*
  • Humans
  • Methylation
  • Protein-Arginine N-Methyltransferases / chemistry
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Signal Transduction

Substances

  • Histones
  • Histone Demethylases
  • Protein-Arginine N-Methyltransferases