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Originally published In Press as doi:10.1074/jbc.M100128200 on February 8, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16348-16355, May 11, 2001
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p300 Coactivates the Adipogenic Transcription Factor CCAAT/Enhancer-binding Protein alpha *

Robin L. Erickson, Nahid Hemati, Sarah E. Ross, and Ormond A. MacDougaldDagger

From the Department of Physiology, University of Michigan Medical School, Ann Arbor, Michigan 48109-0622

Despite the knowledge that CCAAT/enhancer-binding protein alpha  (C/EBPalpha ) plays an important role in preadipocyte differentiation, our understanding of how C/EBPalpha interacts with nuclear proteins to regulate transcription is limited. Based on the hypothesis that evolutionarily conserved regions are functionally important and likely to interact with coactivators, we compared the amino acid sequence of C/EBPalpha from different species (frog to human) and identified four highly conserved regions (CR1-CR4) within the transactivation domain. A series of amino-terminal truncations and internal deletion constructs were made creating forms of C/EBPalpha which lack single or multiple conserved regions. To determine which regions of the C/EBPalpha transactivation domain are important in its ability to induce spontaneous differentiation of 3T3-L1 preadipocytes, we infected preadipocytes with expression vectors encoding the C/EBPalpha conserved region mutants and observed their ability to induce differentiation. We found that CR2 fused to the DNA binding domain is able to induce spontaneous differentiation independent of the other conserved regions. However, CR2 was not necessary for the adipogenic action of C/EBPalpha because a combination of CR1 and CR3 can also induce adipogenesis. Because the transcriptional coactivator p300 participates in the signaling of many transcription factors to the basal transcriptional apparatus, we examined whether functional interaction exists between C/EBPalpha and p300. Cotransfection of p300 with p42C/EBPalpha results in a synergistic increase in leptin promoter activity, indicating that p300 acts as a transcriptional coactivator of C/EBPalpha . Analyses using C/EBPalpha conserved region mutants suggest that multiple regions (CR2 and CR3) of the C/EBPalpha transactivation domain functionally interact with p300.

* This work was supported by Natural Sciences and Engineering Research Council of Canada predoctoral fellowships (to R. L. E. and S. E. R.) and by a grant from the American Diabetes Association and National Institutes of Health Grant DK51563 (to O. A. 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.

Dagger To whom correspondence should be addressed: Dept. of Physiology, 7744 Medical Science Bldg. II, 1301 E. Catherine, Ann Arbor, MI 48109-0622. Tel.: 734-647-7721; Fax: 734-936-8813; E-mail: macdouga@umich.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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