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Originally published In Press as doi:10.1074/jbc.M910259199 on March 15, 2000

J. Biol. Chem., Vol. 275, Issue 21, 16323-16328, May 26, 2000
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The MEF2A Isoform Is Required for Striated Muscle-specific Expression of the Insulin-responsive GLUT4 Glucose Transporter*

Silvia MoraDagger and Jeffrey E. Pessin§

From the Department of Physiology and Biophysics, University of Iowa, Iowa City, Iowa 52242

Previously, we have demonstrated that an MEF2 consensus sequence located between -473/-464 in the human GLUT4 gene was essential for both tissue-specific and hormonal/metabolic regulation of GLUT4 expression (Thai, M. V., Guruswamy, S., Cao, K. T., Pessin, J. E., and Olson, A. L. (1998) J. Biol. Chem. 273, 14285-14292). To identify the specific MEF2 isoform(s) responsible for GLUT4 expression, we studied the pattern of expression of the MEF2 isoforms in insulin-sensitive tissues. Both heart and skeletal muscle were found to express the MEF2A, MEF2C, and MEF2D isoforms but not MEF2B. However, only the MEF2A protein was selectively down-regulated in insulin-deficient diabetes. Co-immunoprecipitation with isoform-specific antibodies revealed that, in the basal state, essentially all of the MEF2A protein was presented as a MEF2A-MEF2D heterodimer without any detectable MEF2A-MEF2A homodimers or MEF2A-MEF2C and MEF2C-MEF2D heterodimers. Electrophoretic mobility shift assays revealed that nuclear extracts from diabetic animals had reduced binding to the MEF2 binding site compared with extracts from control or insulin-treated animals. Furthermore, immunodepletion of the MEF2A-MEF2D complex from control extracts abolished binding to the MEF2 element. However, addition of MEF2A to diabetic nuclear extracts fully restored binding activity to the MEF2 element. These data strongly suggest that the MEF2A-MEF2D heterodimer is selectively decreased in insulin-deficient diabetes and is responsible for hormonally regulated expression of the GLUT4 gene.

* This work was supported in part by Research Grants DK33823 and DK25295 from the National Institutes of Health.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.

Dagger Recipient of a postdoctoral fellowship (Formacion de Personal Investigador) from the Ministerio de Educacion y Cultura, Spain.

§ To whom correspondence should be addressed: Dept. of Physiology and Biophysics, University of Iowa, 51 Newton Rd., Iowa City, IA 52242. Tel.: 319-335-7823; Fax: 319-335-7330; E-mail: jeffrey- pessin{at}uiowa.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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