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Papers In Press, published online ahead of print March 15, 2000
Department of Physiology & Biophysics, The University of Iowa, Iowa City, IA 52242-1109
Corresponding Author: jeffrey-pessin{at}uiowa.edu
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. 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, C and D isoforms but not MEF2B. However, only the MEF2A protein was selectively downregulated 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 to 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. This data strongly suggests that the MEF2A-MEF2D heterodimer is selectively decreased in insulin-deficient diabetes and is responsible for hormonal-regulated expression of the GLUT4 gene
J. Biol. Chem, 10.1074/jbc.M910259199
Submitted on December 20, 1999
Revised on March 10, 2000
Accepted on March 14, 2000
The MEF2A isoform is required for striated muscle-specific expression of the insulin-responsive GLUT4 glucose transporter
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