NDLI: Trans-regulation of histone deacetylase activities through acetylation.

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Trans-regulation of histone deacetylase activities through acetylation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Stavreva, Diana Huang, Suming Fu, Xueqi Luo, Yi Jian, Wei Qiu, Yi Hager, Gordon Bungert, Jörg
Description	Author Affiliation: Luo Y ( Department of Anatomy and Cell Biology, University of Florida, Gainesville, Florida 32610, USA.)
Abstract	HDAC1 and -2 are highly conserved enzymes and often coexist in the same coregulator complexes. Understanding the regulation of histone deacetylase activities is extremely important because these enzymes play key roles in epigenetic regulation in normal and cancer cells. We previously showed that HDAC1 is required for glucocorticoid receptor-mediated transcription activation and that its activity is regulated through acetylation by p300 during the induction cycle. Here, we showed that HDAC2 is also required for glucocorticoid receptor-mediated gene activation. HDAC2, however, is regulated through a different mechanism from that of HDAC1. HDAC2 is not acetylated by p300, although 5 of 6 acetylated lysine residues in HDAC1 are also present in HDAC2. More importantly, the activity of HDAC2 is inhibited by acetylated HDAC1. Additionally, we showed that acetylated HDAC1 can trans-regulate HDAC2 through heterodimerization. Thus, this study uncovered fundamental differences between HDAC1 and HDAC2. It also unveiled a new mechanism of collaborative regulation by HDAC1/2 containing coregulator complexes.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	50
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-12-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Histone Deacetylase 1 Metabolism Histone Deacetylase 2 Receptors, Glucocorticoid Transcriptional Activation Acetylation Amino Acid Sequence Animals Cell Line Genetics Molecular Sequence Data Mutation RNA, Small Interfering Recombinant Fusion Proteins Sequence Alignment P300-CBP Transcription Factors Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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