Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Characterization of a dominant inhibitory E47 protein that suppresses C2C12 myogenesis
Autore:
Becker, JR; Dorman, CR; McClafferty, TM; Johnson, SE;
Indirizzi:
Penn State Univ, Dept Poultry Sci, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 i, University Pk, PA 16802 USA
Titolo Testata:
EXPERIMENTAL CELL RESEARCH
fascicolo: 1, volume: 267, anno: 2001,
pagine: 135 - 143
SICI:
0014-4827(20010701)267:1<135:COADIE>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOOP-HELIX PROTEIN; TRANSCRIPTIONAL ACTIVITIES; HOMODIMER FORMATION; REGULATORY FACTORS; DNA-BINDING; MYOD; E2A; E12; PHOSPHORYLATION; EXPRESSION;
Keywords:
MyoD; myogenin; E47; myogenesis; repression; C2C12;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Johnson, SE Penn State Univ, Dept Poultry Sci, University Pk, PA 16802 USAPenn State Univ University Pk PA USA 16802 y Pk, PA 16802 USA
Citazione:
J.R. Becker et al., "Characterization of a dominant inhibitory E47 protein that suppresses C2C12 myogenesis", EXP CELL RE, 267(1), 2001, pp. 135-143

Abstract

Skeletal muscle formation is controlled through the coordinated actions ofthe muscle regulatory factors (MRFs). The activities of these basic helix-loop-helix proteins is mediated in part through heterodimer formation with a family of ubiquitous bHLH proteins, referred to as E-proteins. The primary E-protein in skeletal muscle is the E2A splice variant, E47. To further address the role of E47 during skeletal myogenesis, we created a chimeric E47 repressor protein by replacing the transcriptional activation domain withthe Drosophila Engrailed transcriptional repressor domain. The dominant inhibitory E-protein (En Delta E47) formed homodimers capable of binding DNA and abolished E47-directed gene transcription. Stable expression of En Delta E47 in mouse C2C12 myoblasts effectively blocked the cells' ability to differentiate into mature myofibers. Closer examination of the molecular basis for the inhibition of myogenesis revealed that En Delta E47 preferentially forms heterodimers with myogenin. Interestingly, the chimeric repressor did not form DNA-binding heterodimers with MyoD in C2C12 myocytes. The failure to detect MyoD:En Delta E47 heterodimers in myoblasts was not due to protein conformational defects as both wild-type E47 and En Delta E47 readily formed DNA binding complexes with MyoD in vitro. These results indicate that E47 plays a crucial role in C2C12 myogenesis by serving as the preferred heterodimer partner of the myogenin protein. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 12:57:09