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J. Biol. Chem., Vol. 279, Issue 44, 45766-45772, October 29, 2004

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Myogenin Protein Stability Is Decreased by BMP-2 through a Mechanism Implicating Id1^*

Francesc Viñals and Francesc Ventura¶

From the Unitat de Bioquímica, Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, E-08907 L'Hospitalet de Llobregat, Spain

Bone morphogenetic protein-2 (BMP-2) induces a switch in differentiation of mesenchymal cells from the myogenic to the osteogenic lineage. Here we describe that in C2C12 cells, BMP-2 decreases myogenin expression induced by des-(1,3) insulin-like growth factor-1 (des-(1,3)IGF-1) or ectopically expressed from a constitutive promoter, even in conditions where myogenin mRNA levels were unaffected. Addition of BMP-2 decreases myogenin protein half-life to 50%, whereas proteasome inhibitors abolish these effects. Forced expression of Id1, either by transient transfection or under the control of an inducible system, causes degradation of myogenin in the absence of BMP-2. In contrast, E47 overexpression blocks the inhibitory effect of BMP-2 on myogenin levels. Finally, expression of E47 in 293 cells stabilizes myogenin, an effect that is dependent on the heterodimerization mediated by their helix-loop-helix. Our findings indicate that induction of Id1 not only blocks transcriptional activity but also induces myogenin degradation by blocking formation of myogenin-E47 protein complexes.

Received for publication, July 16, 2004 , and in revised form, August 4, 2004.

^* This work was supported by Grants BFI2001-2987 and BMC-2002-00737 from the Plan Nacional de Investigación Científica, Desarrollo e Innovación Tecnológica of the Ministerio de Ciencia y Tecnología (to F. Viñals and F. Ventura, respectively) and by a grant from the Generalitat de Catalunya (Distinció de la Generalitat a Joves Investigadors) to F. Ventura. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

Supported by a contract from the Programa Ramón y Cajal of the Ministerio de Ciencia y Tecnología. To whom correspondence may be addressed: Unitat de Bioquímica, Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, C/Feixa Llarga s/n, L'Hospitalet de Llobregat, E-08907 L'Hospitalet de Llobregat, Spain. Tel.: 34-93-402-4281; Fax: 34-93-402-4268; E-mail: fvinals{at}ub.edu.

^¶ To whom correspondence may be addressed: Unitat de Bioquímica, Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, C/Feixa Llarga s/n, L'Hospitalet de Llobregat, E-08907 L'Hospitalet de Llobregat, Spain. Tel.: 34-93-402-4281; Fax: 34-93-402-4268; E-mail: fventura{at}ub.edu.

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