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A more recent version of this article appeared on May 1, 2007
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Submitted on August 31, 2006
Revised on February 14, 2007
Accepted on February 16, 2007
Centre de Recherches de Biochimie Macromoléculaire, Centre National de la Recherche Scientifique, INSERM, 34293 Montpellier, France
Monitoring Editor: Anne Ridley
Cadherins are transmembrane glycoproteins that mediate Ca2+-dependent homophilic cell-cell adhesion and play crucial role during skeletal myogenesis. M-cadherin is required for myoblast fusion into myotubes, but its mechanisms of action remain unknown. The goal of this study was to cast some light on the nature of the M-cadherin-mediated signals involved in myoblast fusion into myotubes. We found that the Rac1 GTPase activity is increased at the time of myoblast fusion and it is required for this process. Moreover, we showed that M-cadherin-dependent adhesion activates Rac1 and demonstrated the formation of a multiproteic complex containing M-cadherin, the Rho-GEF Trio and Rac1 at the onset of myoblast fusion. Interestingly, Trio knockdown efficiently blocked both the increase in Rac1-GTP levels, observed after M-cadherin-dependent contact formation, and myoblast fusion. We conclude that M-cadherin-dependent adhesion can activate Rac1 via the Rho-GEF Trio at the time of myoblast fusion.
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