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J. Biol. Chem., Vol. 282, Issue 2, 956-967, January 12, 2007

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CCAAT/Enhancer-binding Protein (C/EBP) Is Acetylated at Multiple Lysines

ACETYLATION OF C/EBP AT LYSINE 39 MODULATES ITS ABILITY TO ACTIVATE TRANSCRIPTION^*

Teresa I. Ceseña¹, Jean-Rene Cardinaux, Roland Kwok^¶, and Jessica Schwartz^||2

From the Cellular and Molecular Biology Program, the ^¶Departments of Obstetrics/Gynecology and Biological Chemistry and the ^||Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan 48109 and Center for Psychiatric Neuroscience, Department of Psychiatry, University of Lausanne, CH-1008 Prilly-Lausanne, Switzerland

Transcription factor function can be modulated by post-translational modifications. Because the transcription factor CCAAT/enhancer-binding protein (C/EBP) associates with the nuclear coactivator p300, which contains acetyltransferase activity, acetylation of C/EBP was examined to understand its regulation and function. C/EBP is acetylated by acetyltransferases p300 and p300/CREB-binding protein associated factor. Endogenous C/EBP in 3T3-F442A preadipocytes is also recognized by an acetyl-lysine-specific antibody. Analysis of truncations of C/EBP and peptides based on C/EBP sequences identified multiple lysines within C/EBP that can be acetylated. Among these, a novel acetylation site at lysine 39 of C/EBP was identified. Mutation of Lys-39 to arginine or alanine impairs its acetylation and the ability of C/EBP to activate transcription at the promoters for C/EBP and c-fos. Different C/EBP-responsive promoters require different patterns of acetylated lysines in C/EBP for transcription activation. Furthermore, C/EBP acetylation was increased by growth hormone, and mutation of Lys-39 impaired growth hormone-stimulated c-fos promoter activation. These data suggest that acetylation of Lys-39 of C/EBP, alone or in combination with acetylation at other lysines, may play a role in C/EBP-mediated transcriptional activation.

Received for publication, October 21, 2006 , and in revised form, November 9, 2006.

^* This work was supported in part by National Institutes of Health Grant DK46072 (to J. S.), by the Michigan Diabetes Research and Training Center, National Institutes of Health Grant 5P60 DK20572 (to R. K.), and by the Swiss National Science Foundation Grant 31-64031.00 (to J. R. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2 and Table S1.

¹ Supported by National Institutes of Health Cellular and Molecular Biology Training Grant T32-GM07315, National Institutes of Health Predoctoral Fellowship Grant T32-HD07505, a National Science Foundation/Rackham Merit fellowship from the University of Michigan, and National Institutes of Health Predoctoral Fellowship DK074377-01.

² To whom correspondence should be addressed. Tel.: 734-647-2124; Fax: 734-647-9523; E-mail: jeschwar{at}umich.edu.

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