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Histone deacetylases as transducers and targets of nuclear signaling

✍ Scribed by Donald R. Walkinshaw; Soroush Tahmasebi; Nicholas R. Bertos; Xiang-Jiao Yang

Book ID
102302910
Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
309 KB
Volume
104
Category
Article
ISSN
0730-2312

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✦ Synopsis

Abstract

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. Β© 2008 Wiley‐Liss, Inc.

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Histone deacetylases (HDACs) are enzymes that cleave off acetyl groups from acetyl-lysine residues in histones and various nonhistone proteins. Four different classes of HDACs have been identified in humans so far. Although classes I, II, and IV are zinc-dependent amidohydrolases, class III HDACs de