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J. Biol. Chem., Vol. 279, Issue 35, 36795-36802, August 27, 2004

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N-cadherin Activation Substitutes for the Cell Contact Control in Cell Cycle Arrest and Myogenic Differentiation

INVOLVEMENT OF p120 AND -CATENIN^*

Julie Gavard, Véronique Marthiens, Céline Monnet¶, Mireille Lambert, and René Marc Mège||

From the Signalisation et Différenciation Cellulaires dans les Systèmes Nerveux et Musculaire, U440 INSERM/UPMC, Institut du Fer à Moulin, 17 rue du Fer à Moulin, 75005 Paris, France

N-cadherin is expressed throughout skeletal myogenesis and has been proposed to be involved in the differentiation program of myogenic precursors. Here, we further characterize the N-cadherin involvement and its mechanism of action at the onset of differentiation, through controlled N-cadherin activation by plating isolated C2 myoblasts on surfaces coated with a chimeric Ncad-Fc homophilic ligand (N-cadherin ectodomain fused to the immunoglobulin G Fc fragment). We show that N-cadherin activation substitutes for the cell density in myogenic differentiation by promoting myogenin and troponin T expression. In addition, N-cadherin adhesion participates to the associated cell cycle arrest through the nuclear accumulation of cyclin-dependent kinase inhibitors p21 and p27. Mouse primary myoblast cultures exhibited similar responses to N-cadherin as C2 cells. RNA interference knockdowns of the N-cadherin-associated cytoplasmic proteins p120 and -catenin produced opposite effects on the differentiation pathway. p120 silencing resulted in a decreased myogenic differentiation, associated with a reduction in cadherin-catenin content, which may explain its action on myogenic differentiation. -Catenin silencing led to a stimulatory effect on myogenin expression, without any effect on cell cycle. Our results demonstrate that N-cadherin adhesion may account for cell-cell contact-dependent cell cycle arrest and differentiation of myogenic cells, involving regulation through p120 and -catenins.

Received for publication, February 16, 2004 , and in revised form, May 10, 2004.

^* This work was supported by institutional funding from INSERM, as well as by grants from the Association Française contre les Myopathies and the Association Française de Recherche contre le Cancer. 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.

Supported by a graduate student fellowship from the Ministère de la Recherche, Université Pierre et Marie Curie.

Supported by a Association Française contre les Myopathies graduate fellowship.

^¶ Present address: Centre de Physiopathologie de Toulouse Purpan, INSERM U563, CHU, Purpan, Toulouse France.

^|| To whom correspondence should be addressed: INSERM U440, Institut du Fer à Moulin, 17 rue du Fer à Moulin, 75005 Paris, France. Tel.: 33-1-45-87-61-36; Fax: 33-1-45-87-61-32; E-mail: mege{at}fer-a-moulin.inserm.fr.

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