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J Biol Chem, Vol. 274, Issue 8, 5193-5200, February 19, 1999
From the Department of Biochemistry, Rappaport Institute for
Research in the Medical Sciences, Faculty of Medicine, Technion-Israel
Institute of Technology, Haifa 31096, Israel
Differentiation of muscle cells is regulated by
extracellular growth factors that transmit largely unknown signals into
the cells. Some of these growth factors induce mitogen-activated
protein kinase (MAPK) cascades within muscle cells. In this work we
show that the kinase activity of p38 MAPK is induced early during
terminal differentiation of L8 cells. Addition of a specific p38
inhibitor SB 203580 to myoblasts blocked their fusion to multinucleated myotubes and prevented the expression of MyoD and MEF2 family members
and myosin light chain 2. The expression of MKK6, a direct activator of
p38, or of p38 itself enhanced the activity of MyoD in converting
10T1/2 fibroblasts to muscle, whereas treatment with SB 203580 inhibited MyoD. Several lines of evidence suggesting that the
involvement of p38 in MyoD activity is mediated via its co-activator
MEF2C, a known substrate of p38, are presented. In these experiments we
show that MEF2C protein and MEF2-binding sites are necessary for the
p38 MAPK pathway to regulate the transcription of muscle creatine
kinase reporter gene. Our results indicate that the p38 MAPK pathway
promotes skeletal muscle differentiation at least in part via
activation of MEF2C.
p38 Mitogen-activated Protein Kinase Pathway Promotes Skeletal
Muscle Differentiation
PARTICIPATION OF THE MEF2C TRANSCRIPTION FACTOR
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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