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Laboratoire de Biologie Moléculaire et Cellulaire, CNRS UMR 5161, Ecole Normale Supérieure de Lyon, 46 allée d’Italie, 69007 Lyon, France
¹ Endocrinologie Moléculaire et Cellulaire des Cancers, INSERM U540, 60 rue de Navacelles, 34090 Montpellier, France

(Requests for offprints should be addressed to J-M Vanacker; Email : jvanacker{at}valdorel.fnclcc.fr)

BH and JMV are now at Génotype et Phénotypes Tumoraux, INSERM EMI0229, CRLC Val d’Auvelle Paul Lamarque, 34298 Montpellier, France

The estrogen-receptor-related (ERR) receptors are orphan members of the nuclear receptor superfamily that bind to their specific DNA target sites as homodimers. However, it has not been shown whether this mode of binding is required for the transcriptional activation they drive. We here show that heterodimerization can also occur between these receptors. Furthermore, we demonstrate that the unique amphioxus ortholog of ERR genes (AmphiERR) is expressed as two isoforms differing by an in-frame insertion. While the short isoform behaves like its mammalian counterparts, the long isoform (AmphiERR(L)) displays divergent transcriptional properties according to the target site to which it binds. Indeed, AmphiERR(L) binds as a monomer but does not activate transcription through the SF1 response element (SFRE). On the contrary, this isoform binds as a homodimer and activates transcription through the classical estrogen-response element. Our results strongly suggest that dimerization is required for transactivation exerted by the ERR receptors.

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