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Institut National de la Santé et de la Recherche Médicale (INSERM) Unité 540 (A.C., A.H., S.B., S.J., V.C.), Endocrinologie Moléculaire et Cellulaire des Cancers and Université de Montpellier I, 34090 Montpellier, France; and Equipe Mixte INSERM 0229 (J.-M.V.), Centre Régional de Lutte contre le Cancer Val d’Aurelle, 34298 Montpellier, France
Address all correspondence and requests for reprints to: Vincent Cavailles, Institut National de la Santé et de la Recherche Médicale Unité 540, Endocrinologie Moléculaire et Cellulaire des Cancers and Université de Montpellier I, 60 rue de Navacelles, 34090 Montpellier, France. E-mail: v.cavailles{at}montp.inserm.fr.
We have investigated the effects of receptor-interacting protein 140 (RIP140) on transcriptional regulation by estrogen receptor-related receptors (ERRs). We first show that RIP140 inhibits transactivation by ERR
, ß, and 
on natural or artificial reporter genes containing different types of response elements. This repression correlates with a strong in vitro binding between several regions of RIP140 and the three ERR isoforms. Surprisingly, although RIP140 inhibits transactivation of the thyroid hormone receptor- gene by ERRß, it significantly increases its regulation by ERR and ERR. Mutagenesis and transient transfections in SL2 cells indicate that thyroid hormone receptor- promoter expression involved Sp1 sites. In support of this observation, we demonstrate that RIP140 also positively regulates ERRs transactivation of other known Sp1 targets such as the p21 gene. This effect requires the two proximal Sp1 binding sites of the promoter and is partially dependent on the activation function 2 domain of ERRs. Finally, we provide evidences for a role of histone deacetylases in the regulation of p21 promoter by RIP140. Altogether, these data indicate that RIP140 differentially regulates ERR activity depending on the target sequence on the promoters.
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