Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
, 6 (6), 579-89

Histone Deacetylases and Cancer

Affiliations
Review

Histone Deacetylases and Cancer

Bruna Barneda-Zahonero et al. Mol Oncol.

Abstract

Reversible acetylation of histone and non-histone proteins is one of the most abundant post-translational modifications in eukaryotic cells. Protein acetylation and deacetylation are achieved by the antagonistic actions of two families of enzymes, histone acetyltransferases (HATs) and histone deacetylases (HDACs). Aberrant protein acetylation, particularly on histones, has been related to cancer while abnormal expression of HDACs has been found in a broad range of cancer types. Therefore, HDACs have emerged as promising targets in cancer therapeutics, and the development of HDAC inhibitors (HDIs), a rapidly evolving area of clinical research. However, the contributions of specific HDACs to a given cancer type remain incompletely understood. The aim of this review is to summarize the current knowledge concerning the role of HDACs in cancer with special emphasis on what we have learned from the analysis of patient samples.

Figures

Figure 1
Figure 1
Representative scheme of lysine deacetylation by HDACs. In the presence of a water molecule, HDACs catalyze the removal of the acetyl group from lysine regenerating the ϵ‐amino group and releasing an acetate molecule.
Figure 2
Figure 2
Human HDACs superfamily. HDACs are grouped into four different classes according to sequence similarity and homology to yeast proteins. Specific domains present in different members of each HDAC subfamily are represented in the illustrating cartoon.

Similar articles

See all similar articles

Cited by 113 articles

See all "Cited by" articles

Publication types

LinkOut - more resources

Feedback