Point mutated caveolin-3 form (P104L) impairs myoblast differentiation via Akt and p38 signalling reduction, leading to an immature cell signature |
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Authors: | Elena StoppaniStefania Rossi Elisabetta MeacciFabio Penna Paola CostelliArianna Bellucci Fiorella FaggiDaniele Maiolo Eugenio MontiAlessandro Fanzani |
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Institution: | a Department of Biomedical Sciences and Biotechnologies and Interuniversity Institute of Myology (IIM), University of Brescia, Brescia, Italyb Department of Biochemical Sciences, University of Florence, Florence, Italyc Department of Experimental Medicine and Oncology, University of Turin, Turin, Italy |
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Abstract: | Unbalanced levels of caveolin-3 (Cav3) are involved in muscular disorders. In the present study we show that differentiation of immortalized myoblasts is affected by either lack or overexpression of Cav3. Nevertheless, depletion of Cav3 induced by delivery of the dominant-negative Cav3 (P104L) form elicited a more severe phenotype, characterized by the simultaneous attenuation of the Akt and p38 signalling networks, leading to an immature cell and molecular signature. Accordingly, differentiation of myoblasts harbouring Cav3 (P104L) was improved by countering the reduced Akt and p38 signalling network via administration of IGF-1 or trichostatin A. Furthermore, loss of Cav3 correlated with a deregulation of the TGF-β-induced Smad2 and Erk1/2 pathways, confirming that Cav3 controls TGF-β signalling at the plasma membrane. Overall, these data suggest that loss of Cav3, primarily causing attenuation of both Akt and p38 pathways, contributes to impair myoblast fusion. |
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