Abstract
Histone deacetylases (HDACs) and histone acetyl transferases (HATs) are two counteracting enzyme families whose enzymatic activity controls the acetylation state of protein lysine residues, notably those contained in the N-terminal extensions of the core histones. Acetylation of histones affects gene expression through its influence on chromatin conformation. In addition, several non-histone proteins are regulated in their stability or biological function by the acetylation state of specific lysine residues. HDACs intervene in a multitude of biological processes and are part of a multiprotein family in which each member has its specialized functions. In addition, HDAC activity is tightly controlled through targeted recruitment, protein-protein interactions and post-translational modifications. Control of cell cycle progression, cell survival and differentiation are among the most important roles of these enzymes. Since these processes are affected by malignant transformation, HDAC inhibitors were developed as antineoplastic drugs and are showing encouraging efficacy in cancer patients.
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This work was in part supported by a grant from the Ministero per l'Università e la Ricerca Scientifica (MIUR)
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Gallinari, P., Marco, S., Jones, P. et al. HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics. Cell Res 17, 195–211 (2007). https://doi.org/10.1038/sj.cr.7310149
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DOI: https://doi.org/10.1038/sj.cr.7310149
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