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Histone deacetylases: salesmen and customers in the post‐translational modification market
Author(s) -
Brandl André,
Heinzel Thorsten,
Krämer Oliver H.
Publication year - 2009
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1042/bc20080158
Subject(s) - acetylation , sumo protein , histone , histone deacetylase , biology , posttranslational modification , ubiquitin , lysine , microbiology and biotechnology , phosphorylation , biochemistry , computational biology , enzyme , dna , amino acid , gene
HDACs (histone deacetylases) are enzymes that remove the acetyl moiety from N‐∍‐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.