Class IIa histone deacetylases: regulating the regulators

Oncogene. 2007 Aug 13;26(37):5450-67. doi: 10.1038/sj.onc.1210613.

Abstract

In the last decade, the identification of enzymes that regulate acetylation of histones and nonhistone proteins has revealed the key role of dynamic acetylation and deacetylation in various cellular processes. Mammalian histone deacetylases (HDACs), which catalyse the removal of acetyl groups from lysine residues, are grouped into three classes, on the basis of similarity to yeast counterparts. An abundance of experimental evidence has established class IIa HDACs as crucial transcriptional regulators of various developmental and differentiation processes. In the past 5 years, a tremendous effort has been dedicated to characterizing the regulation of these enzymes. In this review, we summarize the latest discoveries in the field and discuss the molecular and structural determinants of class IIa HDACs regulation. Finally, we emphasize that comprehension of the mechanisms underlying class IIa HDAC functions is essential for potential therapeutic applications.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Enzyme Inhibitors / therapeutic use
  • Histone Deacetylases / chemistry*
  • Histone Deacetylases / classification
  • Histone Deacetylases / metabolism*
  • Humans
  • Mice
  • Protein Structure, Tertiary

Substances

  • Enzyme Inhibitors
  • Histone Deacetylases