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MBC in Press, published online ahead of print November 16, 2005
Mol. Biol. Cell 10.1091/mbc.E05-04-0284

A more recent version of this article appeared on February 1, 2006
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Submitted on April 6, 2005
Revised on October 11, 2005
Accepted on November 3, 2005

RhoA GTPase Regulates M-Cadherin Activity and Myoblast Fusion

Sophie Charrasse,* Franck Comunale,* Yaël Grumbach,* Francis Poulat,{dagger} Anne Blangy,* and Cécile Gauthier-Rouvière*

*CRBM, CNRS FRE2593, 34293 Montpellier Cedex, France; {dagger}IGH, CNRS UPR1142, 34396 Montpellier Cedex 5, France

Monitoring Editor: Ben Margolis

The Rho family of GTP-binding proteins plays critical roles during myogenesis induction. To elucidate their role later during myogenesis, we have analyzed RhoA function during myoblast fusion into myotubes. We find that RhoA activity is rapidly and transiently increased when cells are shifted into differentiation medium and then is decreased until myoblast fusion. RhoA activity must be down-regulated to allow fusion, as expression of a constitutively active form of RhoA (RhoAV14) inhibits this process. RhoAV14 perturbs the expression and localization of M-cadherin, a member of the Ca2+-dependent cell-cell adhesion molecule family that has an essential role in skeletal muscle cell differentiation. This mutant does not affect N-cadherin and other proteins involved in myoblast fusion, {beta}1-integrin and ADAM12. Active RhoA induces the entry of M-cadherin into a degradative pathway and thus decreases its stability in correlation with the monoubiquitination of M-cadherin. Moreover, p120 catenin association with M-cadherin is decreased in RhoAV14-expressing cells, which is partially reverted by the inhibition of the RhoA effector Rho-associated kinase ROCK. ROCK inhibition also restores M-cadherin accumulation at the cell-cell contact sites. We propose that the sustained activation of the RhoA pathway inhibits myoblast fusion through the regulation of p120 activity, which controls cadherin internalization and degradation.

Address correspondence to: Cécile Gauthier-Rouvière (cecile.gauthier{at}crbm.cnrs.fr)




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