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J. Biol. Chem., Vol. 282, Issue 52, 37738-37746, December 28, 2007

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Peroxisome Proliferator-activated Receptor (PPAR)-2 Controls Adipocyte Differentiation and Adipose Tissue Function through the Regulation of the Activity of the Retinoid X Receptor/PPAR Heterodimer^*

Péter Bai¹, Sander M. Houten^¶||, Aline Huber, Valérie Schreiber, Mitsuhiro Watanabe^¶, Borbála Kiss, Gilbert de Murcia, Johan Auwerx^¶**, and Josiane Ménissier-de Murcia

From the Département IntégritéduGénome, UMR 7175, CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, BP 10413, Illkirch 67412, France, the ^¶Institut de Génétique et Biologie Moléculaire et Cellulaire, 1 Rue Laurent Fries, BP 10142, Illkirch 67404, France, the Department of Medical Chemistry, Medical and Health Science Center, University of Debrecen, Nagyerdei krt. 98, Pf. 7., Debrecen 4032, Hungary, the ^||Laboratory of Genetic Metabolic Diseases, Academic Medical Center, Amsterdam 1105 AZ, The Netherlands, and the ^**Institut Clinique de la Souris, 1 Rue Laurent Fries, BP 10142, Illkirch 67404, France

The peroxisome proliferator-activated receptor- (PPAR, NR1C3) in complex with the retinoid X receptor (RXR) plays a central role in white adipose tissue (WAT) differentiation and function, regulating the expression of key WAT proteins. In this report we show that poly(ADP-ribose) polymerase-2 (PARP-2), also known as an enzyme participating in the surveillance of the genome integrity, is a member of the PPAR/RXR transcription machinery. PARP-2^-/- mice accumulate less WAT, characterized by smaller adipocytes. In the WAT of PARP-2^-/- mice the expression of a number of PPAR target genes is reduced despite the fact that PPAR1 and -2 are expressed at normal levels. Consistent with this, PARP-2^-/- mouse embryonic fibroblasts fail to differentiate to adipocytes. In transient transfection assays, PARP-2 small interference RNA decreases basal activity and ligand-dependent activation of PPAR, whereas PARP-2 overexpression enhances the basal activity of PPAR, although it does not change the maximal ligand-dependent activation. In addition, we show a DNA-dependent interaction of PARP-2 and PPAR/RXR heterodimer by chromatin immunoprecipitation. In combination, our results suggest that PARP-2 is a novel cofactor of PPAR activity.

Received for publication, February 2, 2007 , and in revised form, September 25, 2007.

This work is dedicated to the memory of Josiane Ménissier-de Murcia, who passed away (July 15, 2007).

^* This work was supported by INSERM, Université Louis Pasteur, the European Union (Grant LSHM-CT-2004-512013), National Institutes of Health Grant DK 067320, Federation of European Biochemical Societies (long term fellowship), CNRS, Association pour la Recherche contre le Cancer, Electricité de France, Ligue contre le Cancer, Commissariat à l'Energie Atomique and Agence Nationale pour la Recherche, Ministère des Affaires Etrangères, Ambassade de la France en Hongrie, and a Bolyai Fellowship of the Hungarian Academy of Sciences (to P. B.). The authors declare no conflict of interest. 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.

¹ To whom correspondence should be addressed. Tel.: 36-52-412-345; Fax: 36-52-412-566; E-mail: baip{at}dote.hu.

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