Deacetylation of nonhistone proteins by HDACs and the implications in cancer

Handb Exp Pharmacol. 2011:206:39-56. doi: 10.1007/978-3-642-21631-2_3.


Acetylation and deacetylation of lysine residues controlled by histone acetyltransferases (HATs) and histone deacetylases (HDACs), respectively, are among the most common posttranslational modifications of proteins. In addition to histones, a large number of nonhistone proteins that can undergo reversible acetylation have been identified. These nonhistone acetylated/deacetylated proteins are involved in a wide range of cellular processes including transcription, translation, DNA repair, metabolism, and cell structure. Aberrant deacetylation of nonhistone proteins is implicated in many human diseases, including cancer. In this chapter, we review and describe the involvement of HDACs in cancer-associated cellular processes via deacetylation of nonhistone proteins, and the possible implications for carcinogenesis and cancer development.

Publication types

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

MeSH terms

  • Acetylation
  • Animals
  • Apoptosis
  • Autophagy
  • Cell Differentiation
  • DNA Damage
  • Histone Acetyltransferases / metabolism
  • Histone Deacetylase Inhibitors / therapeutic use
  • Humans
  • Lysine
  • Neoplasm Invasiveness
  • Neoplasms / enzymology*
  • Neoplasms / immunology
  • Neoplasms / pathology
  • Neoplasms / virology
  • Protein Processing, Post-Translational*


  • Histone Deacetylase Inhibitors
  • Histone Acetyltransferases
  • Lysine