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Nucleic Acids Research, 2000, Vol. 28, No. 16 3168-3177
© 2000 Oxford University Press

Protein kinase-A dependent phosphorylation of transcription enhancer factor-1 represses its DNA-binding activity but enhances its gene activation ability

Mahesh P. Gupta*, Paul Kogut and Madhu Gupta1

Department of Surgery (Cardiac and Thoracic), The University of Chicago, 5841 South Maryland Avenue, Chicago, IL 60637, USA and 1The Hope Children’s Hospital and Department of Physiology and Biophysics, The University of Illinois, Chicago, IL 60612, USA

The cAMP-dependent signaling pathway has been implicated in cardiac cell growth/differentiation and muscle gene transcription. Previously, we have identified a cAMP-inducible E-box/M-CAT hybrid motif in the cardiac {alpha}-myosin heavy chain ({alpha}-MHC) gene promoter. The two factors, TEF-1 and Max, that bind to this motif are found to physically associate with each other and exert a positive cooperative effect for gene regulation. Here we show that TEF-1, but not Max, is a substrate for protein kinase-A (PK-A)-dependent phosphorylation. TEF-1 is phosphorylated by PK-A at residue serine-102. This post-translational modification of TEF-1 repressed its DNA-binding activity, but not its ability to interact with the Max protein. Replacement of serine-102 in TEF-1 by a neutral or a charged amino acid did not abolish its DNA-binding ability, suggesting that changing a charge at the 102 amino-acid position of TEF-1 was not sufficient to inhibit its DNA-binding activity. We also show that PK-A response of the {alpha}-MHC gene is stimulated by the presence of wild-type TEF-1 but not by mutant TEF-1 having serine-102 replaced by alanine, suggesting that phosphorylation at this residue accounts for the cAMP/PK-A response of the gene. Thus, these data demonstrate that TEF-1 is a direct target of cAMP/PK-A signaling in cardiac myocytes.

* To whom correspondence should be addressed. Tel: +1 773 834 4648; Fax: +1 773 702 4187; Email: mgupta@surgery.bsd.uchicago.edu


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