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Molecular and Cellular Biology, June 2000, p. 3951-3964, Vol. 20, No. 11
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

p38 and Extracellular Signal-Regulated Kinases Regulate the Myogenic Program at Multiple Steps

Zhenguo Wu,1,2,dagger Pamela J. Woodring,3,4 Kunjan S. Bhakta,3 Kumiko Tamura,1,2 Fang Wen,2 James R. Feramisco,2,4 Michael Karin,1,2,4 Jean Y. J. Wang,3,4 and Pier Lorenzo Puri3,5,*

Laboratory of Gene Regulation and Signal Transduction,1 Department of Pharmacology,2 Department of Biology,3 and Cancer Center,4 University of California, San Diego, La Jolla, California 92093-0322, and Laboratory of Gene Expression, Fondazione A. Cesalpino, Istituto I Clinica Medica, Policlinico Umberto I, University of Rome, Rome, Italy5

Received 2 December 1999/Returned for modification 10 January 2000/Accepted 10 March 2000

The extracellular signals which regulate the myogenic program are transduced to the nucleus by mitogen-activated protein kinases (MAPKs). We have investigated the role of two MAPKs, p38 and extracellular signal-regulated kinase (ERK), whose activities undergo significant changes during muscle differentiation. p38 is rapidly activated in myocytes induced to differentiate. This activation differs from those triggered by stress and cytokines, because it is not linked to Jun-N-terminal kinase stimulation and is maintained during the whole process of myotube formation. Moreover, p38 activation is independent of a parallel promyogenic pathway stimulated by insulin-like growth factor 1. Inhibition of p38 prevents the differentiation program in myogenic cell lines and human primary myocytes. Conversely, deliberate activation of endogenous p38 stimulates muscle differentiation even in the presence of antimyogenic cues. Much evidence indicates that p38 is an activator of MyoD: (i) p38 kinase activity is required for the expression of MyoD-responsive genes, (ii) enforced induction of p38 stimulates the transcriptional activity of a Gal4-MyoD fusion protein and allows efficient activation of chromatin-integrated reporters by MyoD, and (iii) MyoD-dependent myogenic conversion is reduced in mouse embryonic fibroblasts derived from p38alpha -/- embryos. Activation of p38 also enhances the transcriptional activities of myocyte enhancer binding factor 2A (MEF2A) and MEF2C by direct phosphorylation. With MEF2C, selective phosphorylation of one residue (Thr293) is a tissue-specific activating signal in differentiating myocytes. Finally, ERK shows a biphasic activation profile, with peaks of activity in undifferentiated myoblasts and postmitotic myotubes. Importantly, activation of ERK is inhibitory toward myogenic transcription in myoblasts but contributes to the activation of myogenic transcription and regulates postmitotic responses (i.e., hypertrophic growth) in myotubes.

* Corresponding author. Mailing address: Department of Biology, UCSD, 9500 Gilman Dr., La Jolla, CA 92093-0322. Phone: (858) 534-2828. Fax: (858) 534-2821. E-mail: plorenzo{at}biomail.ucsd.edu.

dagger Present address: Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.

Molecular and Cellular Biology, June 2000, p. 3951-3964, Vol. 20, No. 11
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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