A dynamic role for HDAC7 in MEF2-mediated muscle differentiation

Dressel, Uwe, Bailey, Peter J., Wang, S-C. Mary, Downes, Michael, Evans, Ronald M. and Muscat, George E. O. (2001) A dynamic role for HDAC7 in MEF2-mediated muscle differentiation. Journal of Biological Chemistry, 276 20: 17007-17013. doi:10.1074/jbc.M101508200

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Author Dressel, Uwe
Bailey, Peter J.
Wang, S-C. Mary
Downes, Michael
Evans, Ronald M.
Muscat, George E. O.
Title A dynamic role for HDAC7 in MEF2-mediated muscle differentiation
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2001
Sub-type Article (original research)
DOI 10.1074/jbc.M101508200
Open Access Status File (Publisher version)
Volume 276
Issue 20
Start page 17007
End page 17013
Total pages 7
Place of publication Bethesda
Publisher The American Society for Biochemistry and Molecular Biology
Collection year 2001
Language eng
Subject C1
270100 Biochemistry and Cell Biology
780105 Biological sciences
Abstract The overlapping expression profile of MEF2 and the class-II histone deacetylase, HDAC7, led us to investigate the functional interaction and relationship between these regulatory proteins. HDAC7 expression inhibits the activity of MEF2 (-A, -C, and -D), and in contrast MyoD and Myogenin activities are not affected. Glutathione S-transferase pulldown and immunoprecipitation demonstrate that the repression mechanism involves direct interactions between MEF2 proteins and HDAC7 and is associated with the ability of MEF2 to interact with the N-terminal 121 amino acids of HDAC7 that encode repression domain 1. The MADS domain of MEF2 mediates the direct interaction of MEF2 with HDAC7, MEF2 inhibition by HDAC7 is dependent on the N-terminal repression domain and surprisingly does not involve the C-terminal deacetylase domain. HDAC7 interacts with CtBP and other class-I and -II HDACs suggesting that silencing of MEF2 activity involves corepressor recruitment. Furthermore, we show that induction of muscle differentiation by serum withdrawal leads to the translocation of HDAC7 from the nucleus into the cytoplasm. This work demonstrates that HDAC7 regulates the function of MEF2 proteins and suggests that this class-II HDAC regulates this important transcriptional (and pathophysiological) target in heart and muscle tissue. The nucleocytoplasmic trafficking of HDAC7 and other class-II HDACs during myogenesis provides an ideal mechanism for the regulation of HDAC targets during mammalian development and differentiation.
Keyword Biochemistry & Molecular Biology
Myocyte Enhancer Factor-2
Mef2 Transcription Factor
Myod Gene Family
Skeletal-muscle
Histone Deacetylase-4
Mouse Embryogenesis
Orphan Receptor
Bhlh Proteins
Mads-box
Expression
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Tue, 14 Aug 2007, 15:44:30 EST