title: Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression.
abstract: The flexible N-terminal tails of core histones are subject to dynamic, reversible lysine acetylation. At least 10 histone deacetylases have been identified in Saccharomyces cerevisiae and 19 in humans. Emerging themes regarding the function and regulation of these enzymes include the following: targeted and non-targeted chromatin deacetylation; their collaboration with each other and with other chromatin regulators to promote transcriptional repression and silencing; deacetylation of transcription factors and other non-histone proteins; and regulation by subcellular compartmentalization and subunit association. Histone deacetylases are important targets for drugs with potential therapeutic value in the treatment of cancer, neurodegenerative disorders, cardiac hypertrophy and other human diseases.
authors.affiliation: Molecular Oncology Group, Department of Medicine, McGill University Health Centre, Montréal, Québec H3A 1A1, Canada.
authors.forename: Xiang-Jiao
authors.initials: XJ
authors.lastname: Yang
authors.forename: Edward
authors.initials: E
authors.lastname: Seto
mesh_terms: D002843:Chromatin / Q000378:metabolism*; D005786:Gene Expression Regulation / Q000502:physiology*; D020868:Gene Silencing; D006655:Histone Deacetylases / Q000378:metabolism*; D006801:Humans; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D037761:Sirtuins / Q000378:metabolism; D014404:Tubulin / Q000378:metabolism
chemical_list: D002843:Chromatin; D014404:Tubulin; D037761:Sirtuins; D006655:Histone Deacetylases