title: Histone deacetylases: salesmen and customers in the post-translational modification market.
abstract: HDACs (histone deacetylases) are enzymes that remove the acetyl moiety from N-epsilon-acetylated lysine residues in histones and non-histone proteins. In recent years, it has turned out that HDACs themselves are also subject to post-translational modification. Such structural alterations can determine the stability, localization, activity and protein-protein interactions of HDACs. This subsequently affects the modification of their substrates and the co-ordination of cellular signalling networks. Intriguingly, physiologically relevant non-histone proteins are increasingly found to be deacetylated by HDACs, and aberrant deacetylase activity contributes to several severe human diseases. Targeting the catalytic activity of these enzymes and their post-translational modifications are therefore attractive targets for therapeutical intervention strategies. To achieve this ambitious goal, details on the molecular mechanisms regulating post-translational modifications of HDACs are required. This review summarizes aspects of the current knowledge on the biological role and enzymology of the phosphorylation, acetylation, ubiquitylation and sumoylation of HDACs.
authors.affiliation: Friedrich-Schiller-University Jena, Center for Molecular Biomedicine, Institute of Biochemistry and Biophysics, Hans-Knöll-Str. 2, 07745 Jena, Germany.
authors.forename: André
authors.initials: A
authors.lastname: Brandl
authors.forename: Thorsten
authors.initials: T
authors.lastname: Heinzel
authors.forename: Oliver H
authors.initials: OH
authors.lastname: Krämer
mesh_terms: D000107:Acetylation; D006655:Histone Deacetylases / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D054875:Ubiquitination
chemical_list: D006657:Histones; D007527:Isoenzymes; D006655:Histone Deacetylases