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J. Biol. Chem., Vol. 279, Issue 1, 319-325, January 2, 2004

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Suppressive Effect of Receptor-interacting Protein 140 on Coregulator Binding to Retinoic Acid Receptor Complexes, Histone-modifying Enzyme Activity, and Gene Activation^*

Xinli Hu, Yixin Chen, Mariya Farooqui, Mary C. Thomas, Cheng-Ming Chiang, and Li-Na Wei¶

From the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455 and the Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106

Gene induction by retinoic acid (RA) is suppressed by overexpression of receptor-interacting protein 140 (RIP140). RIP140-mediated suppression was reversed most effectively by overexpressing the coactivator p300/CREB-binding protein-associated factor (P/CAF). Immunoprecipitation demonstrated coexistence of holoreceptors complexed with RIP140 or P/CAF. Chromatin immunoprecipitation revealed rapid RA-enhanced recruitment of RIP140, but delayed P/CAF recruitment, to an RA-targeted promoter in COS-1 cells supplemented with RIP140. In RA-induced P19 cells, endogenous RIP140 was rapidly (within 4 h) and significantly recruited to both the RAR2 and TR2 genes, whereas the peak of endogenous P/CAF recruitment occurred much later (48 h) and to a lesser degree. Consistent with these observations, significant histone acetylation of endogenous RA receptor (RAR) targets was only observed 48 h following RA treatment. In vitro experiments confirmed RA-induced transcription from a chromatin template, which was reduced by adding RIP140. This study presents evidence for coexistence of multiple RAR-coregulator complexes and a preferential RA-induced recruitment of RIP140 to endogenous RAR-targeted promoters after short term RA treatment, which correlates with suppressed induction of RA-regulated gene expression in the presence of RIP140.

Received for publication, July 15, 2003 , and in revised form, October 14, 2003.

^* This work was supported by National Institutes of Health Grants DK54733, DK60521, K02 DA13926, DA11190, and DA11806 (to L.-N. W.) and National Institutes of Health Grants GM59643 and CA81017 (to C.-M. 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.

^¶ To whom correspondence should be addressed: Dept. of Pharmacology, University of Minnesota Medical School, 6-120 Jackson Hall, 321 Church St. S.E., Minneapolis, MN 55455. Tel.: 612-625-9402; Fax: 612-625-8408; E-mail: weixx009{at}tc.umn.edu.

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