Document Detail


Histone deacetylase 3 interacts with and deacetylates myocyte enhancer factor 2.
MedLine Citation:
PMID:  17158926     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The myocyte enhancer factor 2 (MEF2) family of transcription factors is not only important for controlling gene expression in normal cellular programs, like muscle differentiation, T-cell apoptosis, neuronal survival, and synaptic differentiation, but has also been linked to cardiac hypertrophy and other pathological conditions. Lysine acetylation has been shown to modulate MEF2 function, but it is not so clear which deacetylase(s) is involved. We report here that treatment of HEK293 cells with trichostatin A or nicotinamide upregulated MEF2D acetylation, suggesting that different deacetylases catalyze the deacetylation. Related to the trichostatin A sensitivity, histone deacetylase 4 (HDAC4) and HDAC5, two known partners of MEF2, exhibited little deacetylase activity towards MEF2D. In contrast, HDAC3 efficiently deacetylated MEF2D in vitro and in vivo. This was specific, since HDAC1, HDAC2, and HDAC8 failed to do so. While HDAC4, HDAC5, HDAC7, and HDAC9 are known to recognize primarily the MEF2-specific domain, we found that HDAC3 interacts directly with the MADS box. In addition, HDAC3 associated with the acetyltransferases p300 and p300/CBP-associated factor (PCAF) to reverse autoacetylation. Furthermore, the nuclear receptor corepressor SMRT (silencing mediator of retinoid acid and thyroid hormone receptor) stimulated the deacetylase activity of HDAC3 towards MEF2 and PCAF. Supporting the physical interaction and deacetylase activity, HDAC3 repressed MEF2-dependent transcription and inhibited myogenesis. These results reveal an unexpected role for HDAC3 and suggest a novel pathway through which MEF2 activity is controlled in vivo.
Authors:
Serge Grégoire; Lin Xiao; Jianyun Nie; Xiaohong Zhang; Minghong Xu; Jiarong Li; Jiemin Wong; Edward Seto; Xiang-Jiao Yang
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2006-12-11
Journal Detail:
Title:  Molecular and cellular biology     Volume:  27     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2007-01-31     Completed Date:  2007-03-16     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1280-95     Citation Subset:  IM    
Affiliation:
Molecular Oncology Group, Royal Victoria Hospital, McGill University Health Center, 687 Pine Avenue West, Montréal, Quebec H3A 1A1, Canada.
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MeSH Terms
Descriptor/Qualifier:
Acetylation
Animals
Binding Sites
Cell Cycle Proteins / metabolism
Histone Acetyltransferases / metabolism
Histone Deacetylases / metabolism*
Humans
Mice
Models, Genetic
Muscle Development / genetics
Myoblasts / cytology,  enzymology
Myogenic Regulatory Factors / metabolism*
Nuclear Proteins / metabolism
Nuclear Receptor Co-Repressor 1
Protein Binding
Protein Interaction Mapping
Protein Structure, Tertiary
Protein Transport
Repressor Proteins / metabolism
Transcription Factors / metabolism
Transcription, Genetic
p300-CBP Transcription Factors
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Myogenic Regulatory Factors; 0/NCOR1 protein, human; 0/Ncor1 protein, mouse; 0/Nuclear Proteins; 0/Nuclear Receptor Co-Repressor 1; 0/Repressor Proteins; 0/Transcription Factors; 0/myocyte-specific enhancer-binding factor 2; EC 2.3.1.48/Histone Acetyltransferases; EC 2.3.1.48/p300-CBP Transcription Factors; EC 2.3.1.48/p300-CBP-associated factor; EC 3.5.1.98/Histone Deacetylases; EC 3.5.1.98/histone deacetylase 3
Comments/Corrections

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