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J. Biol. Chem., Vol. 277, Issue 19, 16426-16432, May 10, 2002
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From the The role of activating protein-1 (AP-1) in muscle
cells is currently equivocal. While some studies propose that AP-1 is
inhibitory for myogenesis, others implicate a positive role in this
process. We tested whether this variation may be due to different
properties of the AP-1 subunit composition in differentiating cells.
Using Western analysis we show that c-Jun, Fra-2, and JunD are
expressed throughout the time course of differentiation. Phosphatase
assays indicate that JunD and Fra-2 are phosphorylated in muscle cells and that at least two isoforms of each are expressed in muscle cells.
Electrophoretic mobility shift assays combined with antibody supershifts indicate the appearance of Fra-2 as a major component of
the AP-1 DNA binding complex in differentiating cells. In this context
it appears that Fra-2 heterodimerizes with c-Jun and JunD. Studying the
c-jun enhancer in reporter gene assays we observed that the muscle transcription factors MEF2A and MyoD can contribute to
robust transcriptional activation of the c-jun enhancer. In differentiating muscle cells mutation of the MEF2 site reduces transactivation of the c-jun enhancer and MEF2A is the
predominant MEF2 isoform binding to this cis element.
Transcriptional activation of an AP-1 site containing reporter gene
(TRE-Luc) is enhanced under differentiation conditions compared with
growth conditions in C2C12 muscle cells. Further studies indicate that
Fra-2 containing AP-1 complexes can transactivate the MyoD
enhancer/promoter. Thus, an AP-1 complex containing Fra-2 and c-Jun or
JunD is consistent with muscle differentiation, indicating that AP-1
function during myogenesis is dependent on its subunit composition.
Composition and Function of AP-1 Transcription Complexes during
Muscle Cell Differentiation*
,,,,,, and
Department of Biology, York University,
Toronto, Ontario M3J 1P3, Canada, the § Department of
Biological Sciences, Columbia University, New York, New York 10027, and
the ¶ Department of Cell and Developmental Biology, University of
Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104
*
This work was supported by a grant from the NSERC of Canada
and the CIHR (to J. C. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: 327 Farquharson
LSB, York University, 4700 Keele St., Toronto M3J 1P3. Tel.:
416-736-2100 (ext. 30389); Fax: 416-736-5698; E-mail:
jmcderm@yorku.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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