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Originally published In Press as doi:10.1074/jbc.M101806200 on July 26, 2001

J. Biol. Chem., Vol. 276, Issue 39, 36361-36369, September 28, 2001
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Characterization of the Physical Interaction between Estrogen Receptor alpha  and JUN Proteins*

Catherine Teyssier, Karine Belguise, Florence Galtier, and Dany ChalbosDagger

From the Institut National de la Santé et de la Recherche Médicale, Endocrinologie Moléculaire et Cellulaire des Cancers (U 540), 60 Rue de Navacelles, Montpellier 34090, France

Activated estrogen receptor alpha  (ERalpha ) modulates transcription triggered by the transcription factor activator protein-1 (AP-1), which consists of Jun-Jun homodimers and Jun-Fos heterodimers. Previous studies have demonstrated that the interference occurs without binding of ERalpha to DNA but probably results from protein·protein interactions. However, involvement of a direct interaction between ERalpha and AP-1 is still debated. Using glutathione S-transferase pull-down assays, we demonstrated that ERalpha bound directly to c-Jun and JunB but not to FOS family members, in a ligand-independent manner. The interaction could occur when c-Jun was bound onto DNA, as shown in a protein-protein-DNA assay. It implicated the C-terminal part of c-Jun and amino acids 259-302 present in the ERalpha hinge domain. ERalpha but not an ERalpha mutant deleted of amino acids 250-303 (ER241G), also associated with c-Jun in intact cells, in the presence of estradiol, as shown by two-hybrid and coimmunoprecipitation assays. We also show that ERalpha , c-Jun, and the p160 coactivator GRIP1 can form a multiprotein complex in vitro and in intact cells and that the ERalpha ·c-Jun interaction could be crucial for the stability of this complex. VP16-ERalpha and c-Jun, which both interact with GRIP1, had synergistic effect on GAL4-GRIP1-induced transcription in the presence of estradiol, and this synergistic effect was not observed with the ERalpha mutant VP16-ER241G or when c-Fos, which bound GRIP1 but not ERalpha , was used instead of c-Jun. Finally, ER241G was inefficient for regulation of AP-1 activity, and an ERalpha truncation mutant encompassing the hinge domain had a dominant negative effect on ERalpha action. These results altogether demonstrate that ERalpha can bind to c-Jun in vitro and in intact cells and that this interaction, by stabilizing a multiprotein complex containing p160 coactivator, is likely to be involved in estradiol regulation of AP-1 responses.

* This work was supported by INSERM, the Association pour la Recherche sur le Cancer (Grants 1411 and 5444), the French Ministère de la Recherche et de l'Enseignement Supérieur, and la Ligue Nationale contre le Cancer (fellowship to C. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Tel.: 33-4-67-04-37-66; Fax: 33-4-67-54-05-98; E-mail: chalbos@u540.montp.inserm.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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