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Histone deacetylases as transducers and targets of nuclear signaling
Author(s) -
Walkinshaw Donald R.,
Tahmasebi Soroush,
Bertos Nicholas R.,
Yang XiangJiao
Publication year - 2008
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21746
Subject(s) - histone , crosstalk , histone deacetylase , acetylation , chromatin , hdac10 , microbiology and biotechnology , hdac11 , histone deacetylase 5 , lysine , biology , chemistry , biochemistry , physics , dna , amino acid , gene , optics
Histone deacetylase (HDAC) activity was first discovered about 40 years ago, but it was not until the molecular identification of the first HDACs in 1996 that this family of enzymes gained prominence. In addition to histones, HDACs reverse lysine acetylation of various non‐histone proteins located in the nucleus and the cytoplasm. Here, we examine the nuclear roles of these enzymes, with a specific focus on their active crosstalk with different chromatin regulators. J. Cell. Biochem. 104: 1541–1552, 2008. © 2008 Wiley‐Liss, Inc.