H2A-DUBbing the mammalian epigenome: expanding frontiers for histone H2A deubiquitinating enzymes in cell biology and physiology

Int J Biochem Cell Biol. 2014 May:50:161-74. doi: 10.1016/j.biocel.2014.03.004. Epub 2014 Mar 16.

Abstract

Posttranslational modifications of histone H2A through the attachment of ubiquitin or poly-ubiquitin conjugates are common in mammalian genomes and play an important role in the regulation of chromatin structure, gene expression, and DNA repair. Histone H2A deubiquitinases (H2A-DUBs) are a group of structurally diverse enzymes that catalyze the removal ubiquitin from histone H2A. In this review we provide a concise summary of the mechanisms that mediate histone H2A ubiquitination in mammalian cells, and review our current knowledge of mammalian H2A-DUBs, their biochemical activities, and recent developments in our understanding of their functions in mammalian physiology.

Keywords: Chromatin; DNA repair; Deubiquitinase; Histone H2A; Transcriptional regulation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • DNA Repair
  • Epigenomics
  • Histones / metabolism*
  • Humans
  • Protein Processing, Post-Translational*
  • Ubiquitin-Protein Ligases / metabolism*
  • Ubiquitin-Specific Proteases / metabolism*
  • Ubiquitination

Substances

  • Histones
  • Ubiquitin-Protein Ligases
  • Ubiquitin-Specific Proteases