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Papers In Press, published online ahead of print July 26, 2001
J. Biol. Chem, 10.1074/jbc.M101806200
Submitted on February 27, 2001
Revised on July 3, 2001
Accepted on July 25, 2001

Characterization of the physical interaction between estrogen receptor alpha and JUN proteins

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

U540, INSERM, Montpellier 34090

Corresponding Author: chalbos{at}u540.montp.inserm.fr

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 remains still debated. Using GST 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 on 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.


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