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J Biol Chem, Vol. 273, Issue 17, 10436-10444, April 24, 1998
From the The differentiation of muscle cells is controlled
by the MyoD family of transcription factors. This family is regulated
by extracellular growth factors that transmit largely unknown signals into the cells. Here we show that the activity of extracellular signal-regulated protein kinase (ERK), a kinase that is part of the
mitogen-activated protein kinase (MAPK) cascade, is low in myoblasts
and is induced with the onset of terminal differentiation of C2 cells.
ERK activity is also induced in fibroblasts that were modified to
express MyoD, but not in the parental fibroblast cells. Thus, ERK
induction is an intrinsic property of muscle cells. A specific MAPK
kinase inhibitor (PD098059) that was added to C2 cells partially
inhibited the fusion of myoblasts to multinucleated myotubes without
affecting the expression of muscle-specific markers. This inhibitor
blocked the induction of MyoD expression that normally takes place
during terminal differentiation. Two lines of evidence suggest that the
MAPK cascade induces the activity of MyoD: 1) the expression of
constitutively activated forms of MEK1 or Raf1 enhanced the
transcriptional activity of MyoD in 10T1/2 fibroblasts; and 2) the
addition of PD098059 to fibroblast cells expressing a conditional
MyoD-estrogen fusion protein significantly inhibited the expression of
MyoD-responsive genes. Our results indicate that the MAPK pathway is
activated in differentiating muscle cells and that it positively
regulates the expression and activity of MyoD protein.
Mitogen-activated Protein Kinase Pathway Is Involved in the
Differentiation of Muscle Cells
,,
Department of Biochemistry, Rappaport
Institute for Research in the Medical Sciences, Faculty of Medicine,
Technion-Israel Institute of Technology, Haifa 31096, Israel and the
§ Clinical Research Division, Fred Hutchinson Cancer
Research Center, Seattle, Washington 98109
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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