Histone modifying enzymes and cancer: going beyond histones

J Cell Biochem. 2005 Dec 15;96(6):1137-48. doi: 10.1002/jcb.20615.

Abstract

Mutations in the molecular pathways that regulate cell proliferation, differentiation, and cell death all contribute to cancer formation. Enzymes that covalently modify histones affect these pathways by controlling the dynamic remodeling of chromatin structure. This article reviews several connections between histone modifying enzymes and cancer that are likely mediated via both histone and non-histone substrates. We propose that multiple protein modifications, including phosphorylation, methylation, and acetylation, cross regulate one another to coordinate intermolecular signaling, and that miscues in this regulation can lead to oncogenesis.

Publication types

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

MeSH terms

  • Animals
  • Chromatin / chemistry
  • Chromatin / metabolism
  • Histone Acetyltransferases / metabolism
  • Histone Deacetylases / metabolism
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase / metabolism
  • Histones / genetics
  • Histones / metabolism*
  • Humans
  • Models, Biological
  • Neoplasms / metabolism*
  • Phosphorylation
  • Protein Methyltransferases
  • Protein Processing, Post-Translational / genetics
  • Protein Processing, Post-Translational / physiology*
  • Substrate Specificity

Substances

  • Chromatin
  • Histones
  • Histone Methyltransferases
  • Protein Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • Histone Acetyltransferases
  • Histone Deacetylases