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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
36
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pubmed:dateCreated |
2001-9-4
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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.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/R01 CA070297-06A1,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA070297-07,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA070297-08,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA070297-09,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA070297-10,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA070297-11A2,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA070297-12,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA087767-01A2,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA087767-02,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA087767-03,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA087767-04,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA087767-05,
http://linkedlifedata.com/resource/pubmed/grant/R01 CA77350,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK061002-01A1,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK061002-02,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK061002-03,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK061002-04,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK061002-05,
http://linkedlifedata.com/resource/pubmed/grant/R29 CA070297-03,
http://linkedlifedata.com/resource/pubmed/grant/R29 CA070297-05,
http://linkedlifedata.com/resource/pubmed/grant/R29 CA070297-05S1,
http://linkedlifedata.com/resource/pubmed/grant/R56 DK061002-06A1
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Estradiol,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogen Receptor alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Estrogens,
http://linkedlifedata.com/resource/pubmed/chemical/Forkhead Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Estrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tamoxifen,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33554-60
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pubmed:dateRevised |
2010-12-3
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pubmed:meshHeading |
pubmed-meshheading:11435445-Amino Acid Sequence,
pubmed-meshheading:11435445-Animals,
pubmed-meshheading:11435445-Apoptosis,
pubmed-meshheading:11435445-Binding Sites,
pubmed-meshheading:11435445-COS Cells,
pubmed-meshheading:11435445-Cell Cycle,
pubmed-meshheading:11435445-Cell Nucleus,
pubmed-meshheading:11435445-DNA,
pubmed-meshheading:11435445-DNA, Complementary,
pubmed-meshheading:11435445-Estradiol,
pubmed-meshheading:11435445-Estrogen Receptor alpha,
pubmed-meshheading:11435445-Estrogens,
pubmed-meshheading:11435445-Forkhead Transcription Factors,
pubmed-meshheading:11435445-Genes, Reporter,
pubmed-meshheading:11435445-Glutathione Transferase,
pubmed-meshheading:11435445-Humans,
pubmed-meshheading:11435445-Ligands,
pubmed-meshheading:11435445-Molecular Sequence Data,
pubmed-meshheading:11435445-Nuclear Proteins,
pubmed-meshheading:11435445-Plasmids,
pubmed-meshheading:11435445-Protein Binding,
pubmed-meshheading:11435445-Protein Structure, Tertiary,
pubmed-meshheading:11435445-Receptors, Estrogen,
pubmed-meshheading:11435445-Repressor Proteins,
pubmed-meshheading:11435445-Tamoxifen,
pubmed-meshheading:11435445-Transcription Factors,
pubmed-meshheading:11435445-Transcriptional Activation,
pubmed-meshheading:11435445-Tumor Cells, Cultured,
pubmed-meshheading:11435445-Two-Hybrid System Techniques
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pubmed:year |
2001
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pubmed:articleTitle |
Ligand-dependent interaction of estrogen receptor-alpha with members of the forkhead transcription factor family.
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pubmed:affiliation |
Department of Surgery and Molecular Pharmacology, Stanford University School of Medicine, Stanford, California 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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