HATs and HDACs: From Structure, Function and Regulation to Novel Strategies for Therapy and Prevention

Oncogene. 2007 Aug 13;26(37):5310-8. doi: 10.1038/sj.onc.1210599.

Abstract

Acetylation of the epsilon-amino group of a lysine residue was first discovered with histones in 1968, but the responsible enzymes, histone acetyltransferases and deacetylases, were not identified until the mid-1990s. In the past decade, knowledge about this modification has exploded, with targets rapidly expanding from histones to transcription factors and other nuclear proteins, and then to cytoskeleton, metabolic enzymes, and signaling regulators in the cytoplasm. Thus, protein lysine acetylation has emerged as a major post-translational modification to rival phosphorylation. In this issue of Oncogene, 19 articles review various aspects of the enzymes governing lysine acetylation, especially about their intimate links to cancer. To introduce the articles, we highlight here four central themes: (i) multisubunit enzymatic complexes; (ii) non-histone substrates in diverse cellular processes; (iii) interplay of lysine acetylation with other regulatory mechanisms, such as noncoding RNA-mediated gene silencing and activation; and (iv) novel therapeutic strategies and preventive measures to combat cancer and other human diseases.

Publication types

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

MeSH terms

  • Acetylation
  • Enzyme Inhibitors / therapeutic use*
  • Histone Acetyltransferases / antagonists & inhibitors
  • Histone Acetyltransferases / chemistry*
  • Histone Acetyltransferases / metabolism*
  • Histone Deacetylase Inhibitors
  • Histone Deacetylases / chemistry*
  • Histone Deacetylases / metabolism*
  • Humans
  • Lysine / metabolism*
  • Protein Processing, Post-Translational*

Substances

  • Enzyme Inhibitors
  • Histone Deacetylase Inhibitors
  • Histone Acetyltransferases
  • Histone Deacetylases
  • Lysine