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Originally published In Press as doi:10.1074/jbc.M105555200 on July 2, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33554-33560, September 7, 2001
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Ligand-dependent Interaction of Estrogen Receptor-alpha with Members of the Forkhead Transcription Factor Family*

Eric R. Schuur, Alexander V. Loktev, Manju Sharma, Zijie Sun, Richard A. Roth, and Ronald J. WeigelDagger

From the Department of Surgery and Molecular Pharmacology, Stanford University School of Medicine, Stanford, California 94305

Estrogen acting through the estrogen receptor (ER) is able to regulate cell growth and differentiation of a variety of normal tissues and hormone-responsive tumors. Ligand-activated ER binds DNA and transactivates the promoters of estrogen target genes. In addition, ligand-activated ER can interact with other factors to alter the physiology and growth of cells. Using a yeast two-hybrid screen, we have identified an interaction between ERalpha and the proapoptotic forkhead transcription factor FKHR. The ERalpha -FKHR interaction depends on beta -estradiol and is reduced significantly in the absence of hormone or the presence of Tamoxifen. A glutathione S-transferase pull-down assay was used to confirm the interaction and localized two interaction sites, one in the forkhead domain and a second in the carboxyl terminus. The FKHR interaction was specific to ERalpha and was not detected with other ligand-activated steroid receptors. The related family members, FKHRL1 and AFX, also bound to ERalpha in the presence of beta -estradiol. FKHR augmented ERalpha transactivation through an estrogen response element. Conversely, ERalpha repressed FKHR-mediated transactivation through an insulin response sequence, and cell cycle arrest induced by FKHRL1 in MCF7 cells was abrogated by estradiol. These results suggest a novel mechanism of estrogen action that involves regulation of the proapoptotic forkhead transcription factors.

* This work was supported in part by National Institutes of Health Grant R01 CA77350.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 Supported by a George HA Clowes, MD, FACS, Memorial Research Career Development Award through the American College of Surgeons. To whom correspondence should be addressed: Medical School Laboratory Surge Room P214, 1201 Welch Road, Stanford University School of Medicine, Stanford, CA 94305; Tel.: 650-723-9799; Fax: 650-724-3229; E-mail: ronald. weigel{at}stanford.edu.

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


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