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First published on January 3, 2006; DOI: 10.1124/mol.105.017376

0026-895X/06/6904-1338-1346$20.00
Mol Pharmacol 69:1338-1346, 2006

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Transcriptional Regulation of the Human NRIP1/RIP140 Gene by Estrogen Is Modulated by Dioxin Signalling

Patrick Augereau, Eric Badia, Maryse Fuentes, Fanja Rabenoelina, Marine Corniou, Danièle Derocq, Patrick Balaguer, and Vincent Cavailles

Institut National de la Santé et de la Recherche Médicale, U540, Montpellier, France; and Université Montpellier, Montpellier, France

Receptor interacting protein 140 (RIP140) is a negative transcriptional regulator of nuclear hormone receptors that is required for the maintenance of energy homeostasis and ovulation. In this study, we investigated the mechanisms by which RIP140 expression is controlled by estrogens in breast cancer cells. We first analyzed by real time reverse transcription-polymerase chain reaction the regulation of RIP140 mRNA accumulation by estrogen receptor (ER) ligands in MCF-7 cells. We showed that the induction by estradiol (E2) was rapid and did not affect the apparent stability of the mRNA, suggesting a direct transcriptional regulation. To further study the underlying regulatory mechanisms, we then characterized the human RIP140 gene. We identified several noncoding exons with alternative splicing and localized the promoter region more than 100 kilobases upstream from the coding exon. Although we mapped a perfect consensus estrogen response element able to bind ER{alpha} in gel shift and in chromatin immunoprecipitation experiments, the effect of E2 on RIP140 gene transcription was very modest. This might result at least in part from the presence of an overlapping aryl hydrocarbon receptor (AhR) binding site, which interfered with the E2 response on both the transiently transfected reporter construct and the accumulation of the endogenous RIP140 mRNA. Altogether, our data indicate that the RIP140 gene exhibits a complex structure with several noncoding exons and supports transcriptional cross-talk and feedback involving the ER{alpha} and AhR nuclear receptors.

Received July 27, 2005; accepted January 3, 2006

Address correspondence to: Dr. V. Cavaillès, INSERM, U540, 60 rue de Navacelles, Montpellier, F-34090 France. E-mail: v.cavailles{at}montp.inserm.fr




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