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Titolo:
A dynamic role for HDAC7 in MEF2-mediated muscle differentiation
Autore:
Dressel, U; Bailey, PJ; Wang, SCM; Downes, M; Evans, RM; Muscat, GEO;
Indirizzi:
Univ Queensland, Inst Mol Biosci, Richie Res Lab, Ctr Cellular & Mol Biol,St Lucia, Qld 4072, Australia Univ Queensland St Lucia Qld Australia 4072 St Lucia, Qld 4072, Australia Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 em & Mol Pharmacol, Boston, MA 02115 USA Salk Inst, Howard Hughes Med Inst, Gene Express Lab, San Diego, CA 92186 USA Salk Inst San Diego CA USA 92186 ene Express Lab, San Diego, CA 92186 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 20, volume: 276, anno: 2001,
pagine: 17007 - 17013
SICI:
0021-9258(20010518)276:20<17007:ADRFHI>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
MYOCYTE ENHANCER FACTOR-2; MEF2 TRANSCRIPTION FACTOR; MYOD GENE FAMILY; SKELETAL-MUSCLE; HISTONE DEACETYLASE-4; MOUSE EMBRYOGENESIS; ORPHAN RECEPTOR; BHLH PROTEINS; MADS-BOX; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Muscat, GEO Univ Queensland, Inst Mol Biosci, Richie Res Lab, Ctr Cellular& Mol Biol,B402A, St Lucia, Qld 4072, Australia Univ Queensland B402A St Lucia Qld Australia 4072 2, Australia
Citazione:
U. Dressel et al., "A dynamic role for HDAC7 in MEF2-mediated muscle differentiation", J BIOL CHEM, 276(20), 2001, pp. 17007-17013

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. HDDC7 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 tointeract 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 suggestingthat 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 22:08:54