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Originally published In Press as doi:10.1074/jbc.M201429200 on May 7, 2002

J. Biol. Chem., Vol. 277, Issue 31, 27606-27612, August 2, 2002
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Conserved Amino Acids within CCAAT Enhancer-binding Proteins (C/EBPalpha and beta ) Regulate Phosphoenolpyruvate Carboxykinase (PEPCK) Gene Expression*

Luis A. JuradoDagger §, Shulan SongDagger §, William J. Roesler||, and Edwards A. ParkDagger **

From the Dagger  Department of Pharmacology, College of Medicine, University of Tennessee Health Science Center, Memphis, Tennessee 38163 and the || Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada

Thyroid hormone and cAMP stimulate transcription of the gene for phosphoenolpyruvate carboxykinase (PEPCK). CCAAT enhancer-binding proteins (C/EBPalpha and beta ) are involved in multiple aspects of the nutritional, developmental and hormonal regulation of PEPCK gene expression. Previously, we have identified a thyroid hormone response element in the PEPCK promoter and demonstrated that C/EBP proteins bound to the P3(I) site are participants in the induction of PEPCK gene expression by thyroid hormone and cAMP. Here, we identify several peptide regions within the transactivation domain of C/EBPalpha that enhance the ability of T3 to stimulate gene transcription. We also demonstrate that several conserved amino acids in the transactivation domain of C/EBPalpha and C/EBPbeta are required for the stimulation of basal gene expression and identify amino acids within C/EBPbeta that participate in the cAMP induction of the PEPCK gene. Finally, we show that the CREB-binding protein (CBP) enhanced the induction of PEPCK gene transcription by thyroid hormone and that CBP is associated with the PEPCK gene in vivo. Our results indicate that both C/EBP proteins and CBP participate in the regulation of PEPCK gene transcription by thyroid hormone.

* This work was supported by grants from the American Diabetes Association (to E. A. P.), the Juvenile Diabetes Research Foundation (to E. A. P.), and the Canadian Institute of Health Research (to W. J. R.).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.

§ These authors contributed equally to this work.

Supported by a training grant from the National Institutes of Health.

** To whom correspondence should be addressed: Dept. of Pharmacology, University of Tennessee, College of Medicine, 874 Union Ave., Memphis, TN 38163. Tel.: 901-448-4779; Fax: 901-448-7300; E-mail: epark@utmem.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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