| pubmed-article:11435445 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11435445 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:11435445 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:11435445 | lifeskim:mentions | umls-concept:C0014939 | lld:lifeskim |
| pubmed-article:11435445 | lifeskim:mentions | umls-concept:C0118111 | lld:lifeskim |
| pubmed-article:11435445 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11435445 | pubmed:issue | 36 | lld:pubmed |
| pubmed-article:11435445 | pubmed:dateCreated | 2001-9-4 | lld:pubmed |
| pubmed-article:11435445 | pubmed:abstractText | 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 ER alpha and the proapoptotic forkhead transcription factor FKHR. The ER alpha-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 ER alpha and was not detected with other ligand-activated steroid receptors. The related family members, FKHRL1 and AFX, also bound to ER alpha in the presence of beta-estradiol. FKHR augmented ER alpha transactivation through an estrogen response element. Conversely, ER alpha 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. | lld:pubmed |
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| pubmed-article:11435445 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11435445 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11435445 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11435445 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11435445 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11435445 | pubmed:author | pubmed-author:RothR ARA | lld:pubmed |
| pubmed-article:11435445 | pubmed:author | pubmed-author:SharmaMM | lld:pubmed |
| pubmed-article:11435445 | pubmed:author | pubmed-author:WeigelR JRJ | lld:pubmed |
| pubmed-article:11435445 | pubmed:author | pubmed-author:SunZZ | lld:pubmed |
| pubmed-article:11435445 | pubmed:author | pubmed-author:SchuurE RER | lld:pubmed |
| pubmed-article:11435445 | pubmed:author | pubmed-author:LoktevA VAV | lld:pubmed |
| pubmed-article:11435445 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11435445 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:11435445 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11435445 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11435445 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11435445 | pubmed:pagination | 33554-60 | lld:pubmed |
| pubmed-article:11435445 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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| pubmed-article:11435445 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11435445 | pubmed:articleTitle | Ligand-dependent interaction of estrogen receptor-alpha with members of the forkhead transcription factor family. | lld:pubmed |
| pubmed-article:11435445 | pubmed:affiliation | Department of Surgery and Molecular Pharmacology, Stanford University School of Medicine, Stanford, California 94305, USA. | lld:pubmed |
| pubmed-article:11435445 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11435445 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11435445 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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