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Am J Physiol Cell Physiol 284: C658-C666, 2003. First published November 20, 2002; doi:10.1152/ajpcell.00078.2002
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Vol. 284, Issue 3, C658-C666, March 2003

Regulation of C2C12 myogenic terminal differentiation by MKK3/p38alpha pathway

Candice Cabane*, Walter Englaro*, Karen Yeow, Michel Ragno, and Benoît Dérijard

Unité Mixte de Recherche Centre National de la Recherche Scientifique 6548, Laboratoire de Physiologie Cellulaire et Moléculaire, Faculté des Sciences, Université de Nice-Sophia Antipolis, 06108 Nice cedex 2, France

The signal transduction pathways connecting cell surface receptors to the activation of muscle-specific promoters and leading to myogenesis are still largely unknown. Recently, a contribution of the p38 mitogen-activated protein kinase (MAPK) pathway to this process was evoked through the use of pharmacological inhibitors. We used several mutants of the kinases composing this pathway to modulate the activity of the muscle-specific myosin light chain and myogenin promoters in C2C12 cells by transient transfections. In addition, we show for the first time, using a stable C2C12 cell line expressing a dominant-negative form of the p38 activator MAPK kinase (MKK)3, that a functional p38 MAPK pathway is indeed required for terminal muscle cell differentiation. The most obvious phenotype of this cell line, besides the inhibition of the activation of p38, is its inability to undergo terminal differentiation. This phenotype is accompanied by a drastic inhibition of cell cycle and myogenesis markers such as p21, p27, MyoD, and troponin T, as well as a profound disorganization of the cytoskeleton.

mitogen-activated protein kinase; mitogen-activated protein kinase kinase 3 dominant-negative mutant; muscle; signaling; cytoskeleton

* C. Cabane and W. Englaro contributed equally to this work.




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