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J. Biol. Chem., Vol. 276, Issue 38, 35684-35692, September 21, 2001
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From the Department of Pharmacology and Molecular Cancer Biology,
Duke University Medical Center, Durham, North Carolina 27710
The human estrogen receptor
The Human Estrogen Receptor-
Is a Ubiquitinated Protein
Whose Stability Is Affected Differentially by Agonists, Antagonists,
and Selective Estrogen Receptor Modulators*
-isoform (ER)
is a nuclear transcription factor that displays a complex pharmacology.
In addition to classical agonists and antagonists, the transcriptional
activity of ER can be regulated by selective estrogen receptor
modulators, a new class of drugs whose relative
agonist/antagonist activity is determined by cell context. It has been
demonstrated that the binding of different ligands to ER results in
the formation of unique ER-ligand conformations. These conformations
have been shown to influence ER-cofactor binding and, therefore,
have a profound impact on ER pharmacology. In this study, we
demonstrate that the nature of the bound ligand also influences the
stability of ER, revealing an additional mechanism by which the
pharmacological activity of a compound is determined. Of note we found
that although all ER-ligand complexes can be ubiquitinated and
degraded by the 26 S proteasome in vivo, the mechanisms by
which they are targeted for proteolysis appear to be different.
Specifically, for agonist-activated ER, an inverse relationship
between transcriptional activity and receptor stability was observed.
This relationship does not extend to selective estrogen receptor
modulators and pure antagonists. Instead, it appears that with these
compounds, the determinant of receptor stability is the ligand-induced
conformation of ER. We conclude that the different conformational
states adopted by ER in the presence of different ligands influence
transcriptional activity directly by regulating cofactor binding and
indirectly by modulating receptor stability.
*
This work was supported by National Institutes of Health
Grant DK 48807 (to D. P. M.).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.
To whom correspondence should be addressed: Dept. of Pharmacology
and Molecular Cancer Biology, Duke University Medical Center, Box 3813, Durham, NC 27710. Tel.: 919-684-6035; Fax: 919-681-7139; E-mail:
mcdon016@acpub.duke.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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M. Wormke, M. Stoner, B. Saville, K. Walker, M. Abdelrahim, R. Burghardt, and S. Safe The Aryl Hydrocarbon Receptor Mediates Degradation of Estrogen Receptor {alpha} through Activation of Proteasomes Mol. Cell. Biol., March 15, 2003; 23(6): 1843 - 1855. [Abstract] [Full Text] [PDF]
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V. C. Jordan Is Tamoxifen the Rosetta Stone for Breast Cancer? J Natl Cancer Inst, March 5, 2003; 95(5): 338 - 340. [Full Text] [PDF]
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T. Doi, K. Kinoshita, M. Ikegawa, M. Muramatsu, and T. Honjo Inaugural Article: De novo protein synthesis is required for the activation-induced cytidine deaminase function in class-switch recombination PNAS, March 4, 2003; 100(5): 2634 - 2638. [Abstract] [Full Text] [PDF]
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C. Qin, R. Burghardt, R. Smith, M. Wormke, J. Stewart, and S. Safe Peroxisome Proliferator-activated Receptor {gamma} Agonists Induce Proteasome-dependent Degradation of Cyclin D1 and Estrogen Receptor {alpha} in MCF-7 Breast Cancer Cells Cancer Res., March 1, 2003; 63(5): 958 - 964. [Abstract] [Full Text] [PDF]
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M. Fan, R. M. Bigsby, and K. P. Nephew The NEDD8 Pathway Is Required for Proteasome-Mediated Degradation of Human Estrogen Receptor (ER)-{alpha} and Essential for the Antiproliferative Activity of ICI 182,780 in ER{alpha}-Positive Breast Cancer Cells Mol. Endocrinol., March 1, 2003; 17(3): 356 - 365. [Abstract] [Full Text] [PDF]
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S. T. Pearce, H. Liu, and V. C. Jordan Modulation of Estrogen Receptor alpha Function and Stability by Tamoxifen and a Critical Amino Acid (Asp-538) in Helix 12 J. Biol. Chem., February 21, 2003; 278(9): 7630 - 7638. [Abstract] [Full Text] [PDF]
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 C. Stirone, S. P. Duckles, and D. N. Krause Multiple forms of estrogen receptor-alpha in cerebral blood vessels: regulation by estrogen Am J Physiol Endocrinol Metab, January 1, 2003; 284(1): E184 - E192. [Abstract] [Full Text] [PDF]
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B. A. Kalman and R. L. Spencer Rapid Corticosteroid-Dependent Regulation of Mineralocorticoid Receptor Protein Expression in Rat Brain Endocrinology, November 1, 2002; 143(11): 4184 - 4195. [Abstract] [Full Text] [PDF]
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H. Abdel-Hafiz, G. S. Takimoto, L. Tung, and K. B. Horwitz The Inhibitory Function in Human Progesterone Receptor N Termini Binds SUMO-1 Protein to Regulate Autoinhibition and Transrepression J. Biol. Chem., September 6, 2002; 277(37): 33950 - 33956. [Abstract] [Full Text] [PDF]
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D. B. DeFranco Navigating Steroid Hormone Receptors through the Nuclear Compartment Mol. Endocrinol., July 1, 2002; 16(7): 1449 - 1455. [Abstract] [Full Text] [PDF]
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R. C. Dardes, R. M. O'Regan, C. Gajdos, S. P. Robinson, D. Bentrem, A. De Los Reyes, and V. C. Jordan Effects of a New Clinically Relevant Antiestrogen (GW5638) Related to Tamoxifen on Breast and Endometrial Cancer Growth in Vivo Clin. Cancer Res., June 1, 2002; 8(6): 1995 - 2001. [Abstract] [Full Text] [PDF]
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E. V. Jensen, G. Cheng, C. Palmieri, S. Saji, S. Makela, S. Van Noorden, T. Wahlstrom, M. Warner, R. C. Coombes, and J.-A. Gustafsson Estrogen receptors and proliferation markers in primary and recurrent breast cancer PNAS, November 29, 2001; (2001) 211556298. [Abstract] [Full Text] [PDF]
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E. V. Jensen, G. Cheng, C. Palmieri, S. Saji, S. Makela, S. Van Noorden, T. Wahlstrom, M. Warner, R. C. Coombes, and J.-A. Gustafsson Estrogen receptors and proliferation markers in primary and recurrent breast cancer PNAS, December 18, 2001; 98(26): 15197 - 15202. [Abstract] [Full Text] [PDF]
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