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Vol. 10, Issue 2, 471-486, February 1999

Direct Visualization of the Human Estrogen Receptor alpha  Reveals a Role for Ligand in the Nuclear Distribution of the Receptor

Han Htun,*dagger Dagger Laurel T. Holth,Dagger § Dawn Walker,* James R. Davie,§ and Gordon L. Hager*parallel

 *Laboratory of Receptor Biology and Gene Expression, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892; and  §Department of Biochemistry and Molecular Biology, University of Manitoba, Winnipeg, Manitoba, Canada R3E 0W3

The human estrogen receptor alpha  (ER alpha ) has been tagged at its amino terminus with the S65T variant of the green fluorescent protein (GFP), allowing subcellular trafficking and localization to be observed in living cells by fluorescence microscopy. The tagged receptor, GFP-ER, is functional as a ligand-dependent transcription factor, responds to both agonist and antagonist ligands, and can associate with the nuclear matrix. Its cellular localization was analyzed in four human breast cancer epithelial cell lines, two ER+ (MCF7 and T47D) and two ER- (MDA-MB-231 and MDA-MB-435A), under a variety of ligand conditions. In all cell lines, GFP-ER is observed only in the nucleus in the absence of ligand. Upon the addition of agonist or antagonist ligand, a dramatic redistribution of GFP-ER from a reticular to punctate pattern occurs within the nucleus. In addition, the full antagonist ICI 182780 alters the nucleocytoplasmic compartmentalization of the receptor and causes partial accumulation in the cytoplasm in a process requiring continued protein synthesis. GFP-ER localization varies between cells, despite being cultured and treated in a similar manner. Analysis of the nuclear fluorescence intensity for variation in its frequency distribution helped establish localization patterns characteristic of cell line and ligand. During the course of this study, localization of GFP-ER to the nucleolar region is observed for ER- but not ER+ human breast cancer epithelial cell lines. Finally, our work provides a visual description of the "unoccupied" and ligand-bound receptor and is discussed in the context of the role of ligand in modulating receptor activity.


Dagger    These authors contributed equally to this work.
parallel    Corresponding author. E-mail address: hagerg{at}exchange.nih.gov.
dagger    Present address: Departments of Obstetrics and Gynecology and Molecular and Medical Pharmacology, 27-139 CHS, University of California Los Angeles School of Medicine, 10833 Le Conte Avenue, Los Angeles, CA 90095-1740.


Molecular Biology of the Cell
Vol. 10, 471-486, February 1999
Copyright © 1999 by The American Society for Cell Biology



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Mol. Endocrinol.Home page
C. Pasqualini, D. Guivarc'h, J.-V. Barnier, B. Guibert, J.-D. Vincent, and P. Vernier
Differential Subcellular Distribution and Transcriptional Activity of {{Sigma}}E3, {{Sigma}}E4, and {{Sigma}}E3-4 Isoforms of the Rat Estrogen Receptor-{{alpha}}
Mol. Endocrinol., June 1, 2001; 15(6): 894 - 908.
[Abstract] [Full Text] [PDF]


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Mol Hum ReprodHome page
K. Fukunaka, T. Saito, K. Wataba, K. Ashihara, E. Ito, and R. Kudo
Changes in expression and subcellular localization of nuclear retinoic acid receptors in human endometrial epithelium during the menstrual cycle
Mol. Hum. Reprod., May 1, 2001; 7(5): 437 - 446.
[Abstract] [Full Text] [PDF]


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EndocrinologyHome page
R. H. Price Jr., C. A. Butler, P. Webb, R. Uht, P. Kushner, and R. J. Handa
A Splice Variant of Estrogen Receptor {beta} Missing Exon 3 Displays Altered Subnuclear Localization and Capacity for Transcriptional Activation
Endocrinology, May 1, 2001; 142(5): 2039 - 2049.
[Abstract] [Full Text]


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Mol. Endocrinol.Home page
C. T. Baumann, H. Ma, R. Wolford, J. C Reyes, P. Maruvada, C. Lim, P. M. Yen, M. R. Stallcup, and G. L. Hager
The Glucocorticoid Receptor Interacting Protein 1 (GRIP1) Localizes in Discrete Nuclear Foci That Associate with ND10 Bodies and Are Enriched in Components of the 26S Proteasome
Mol. Endocrinol., April 1, 2001; 15(4): 485 - 500.
[Abstract] [Full Text]


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Mol. Endocrinol.Home page
C. F. Bunn, J. A. Neidig, K. E. Freidinger, T. A. Stankiewicz, B. S. Weaver, J. McGrew, and L. A. Allison
Nucleocytoplasmic Shuttling of the Thyroid Hormone Receptor {{alpha}}
Mol. Endocrinol., April 1, 2001; 15(4): 512 - 533.
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Cancer Res.Home page
C. W. Gregory, R. T. Johnson Jr., J. L. Mohler, F. S. French, and E. M. Wilson
Androgen Receptor Stabilization in Recurrent Prostate Cancer Is Associated with Hypersensitivity to Low Androgen
Cancer Res., April 1, 2001; 61(7): 2892 - 2898.
[Abstract] [Full Text]


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Mol. Endocrinol.Home page
F. Schaufele, C.-y. Chang, W. Liu, J. D. Baxter, S. K. Nordeen, Y. Wan, R. N. Day, and D. P. McDonnell
Temporally Distinct and Ligand-Specific Recruitment of Nuclear Receptor-Interacting Peptides and Cofactors to Subnuclear Domains Containing the Estrogen Receptor
Mol. Endocrinol., December 1, 2000; 14(12): 2024 - 2039.
[Abstract] [Full Text]


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Mol. Endocrinol.Home page
D. M. Ozanne, M. E. Brady, S. Cook, L. Gaughan, D. E. Neal, and C. N. Robson
Androgen Receptor Nuclear Translocation Is Facilitated by the f-Actin Cross-Linking Protein Filamin
Mol. Endocrinol., October 1, 2000; 14(10): 1618 - 1626.
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J. Clin. Endocrinol. Metab.Home page
T. A. Ishunina, F. P. M. Kruijver, R. Balesar, and D. F. Swaab
Differential Expression of Estrogen Receptor {alpha} and {beta} Immunoreactivity in the Human Supraoptic Nucleus in Relation to Sex and Aging
J. Clin. Endocrinol. Metab., September 1, 2000; 85(9): 3283 - 3291.
[Abstract] [Full Text]


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Mol. Endocrinol.Home page
R. K. Tyagi, Y. Lavrovsky, S. C. Ahn, C. S. Song, B. Chatterjee, and A. K. Roy
Dynamics of Intracellular Movement and Nucleocytoplasmic Recycling of the Ligand-Activated Androgen Receptor in Living Cells
Mol. Endocrinol., August 1, 2000; 14(8): 1162 - 1174.
[Abstract] [Full Text]


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Proc. Natl. Acad. Sci. USAHome page
J. Llopis, S. Westin, M. Ricote, J. Wang, C. Y. Cho, R. Kurokawa, T.-M. Mullen, D. W. Rose, M. G. Rosenfeld, R. Y. Tsien, et al.
Ligand-dependent interactions of coactivators steroid receptor coactivator-1 and peroxisome proliferator-activated receptor binding protein with nuclear hormone receptors can be imaged in live cells and are required for transcription
PNAS, April 11, 2000; 97(8): 4363 - 4368.
[Abstract] [Full Text] [PDF]


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Mol. Endocrinol.Home page
D. L. Stenoien, M. G. Mancini, K. Patel, E. A. Allegretto*, C. L. Smith, and M. A. Mancini
Subnuclear Trafficking of Estrogen Receptor-{alpha} and Steroid Receptor Coactivator-1
Mol. Endocrinol., April 1, 2000; 14(4): 518 - 534.
[Abstract] [Full Text]


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Mol. Endocrinol.Home page
S. Oesterreich, Q. Zhang, T. Hopp, S. A. W. Fuqua, M. Michaelis, H. H. Zhao, J. R. Davie, C. K. Osborne, and A. V. Lee
Tamoxifen-Bound Estrogen Receptor (ER) Strongly Interacts with the Nuclear Matrix Protein HET/SAF-B, a Novel Inhibitor of ER-Mediated Transactivation
Mol. Endocrinol., March 1, 2000; 14(3): 369 - 381.
[Abstract] [Full Text]


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J. Cell Sci.Home page
H Poukka, U Karvonen, N Yoshikawa, H Tanaka, J. Palvimo, and O. Janne
The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor
J. Cell Sci., January 9, 2000; 113(17): 2991 - 3001.
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J. Biol. Chem.Home page
K. Prufer, A. Racz, G. C. Lin, and J. Barsony
Dimerization with Retinoid X Receptors Promotes Nuclear Localization and Subnuclear Targeting of Vitamin D Receptors
J. Biol. Chem., December 22, 2000; 275(52): 41114 - 41123.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
X. Cheng and G. W. Hart
Alternative O-Glycosylation/O-Phosphorylation of Serine-16 in Murine Estrogen Receptor beta . POST-TRANSLATIONAL REGULATION OF TURNOVER AND TRANSACTIVATION ACTIVITY
J. Biol. Chem., March 23, 2001; 276(13): 10570 - 10575.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
C. T. Baumann, P. Maruvada, G. L. Hager, and P. M. Yen
Nuclear Cytoplasmic Shuttling by Thyroid Hormone Receptors. MULTIPLE PROTEIN INTERACTIONS ARE REQUIRED FOR NUCLEAR RETENTION
J. Biol. Chem., March 30, 2001; 276(14): 11237 - 11245.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
A. L. Wijayaratne and D. P. McDonnell
The Human Estrogen Receptor-alpha Is a Ubiquitinated Protein Whose Stability Is Affected Differentially by Agonists, Antagonists, and Selective Estrogen Receptor Modulators
J. Biol. Chem., September 14, 2001; 276(38): 35684 - 35692.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
A. Tomura, K. Goto, H. Morinaga, M. Nomura, T. Okabe, T. Yanase, R. Takayanagi, and H. Nawata
The Subnuclear Three-dimensional Image Analysis of Androgen Receptor Fused to Green Fluorescence Protein
J. Biol. Chem., July 20, 2001; 276(30): 28395 - 28401.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
J.-M. Sun, H. Y. Chen, and J. R. Davie
Effect of Estradiol on Histone Acetylation Dynamics in Human Breast Cancer Cells
J. Biol. Chem., December 21, 2001; 276(52): 49435 - 49442.
[Abstract] [Full Text] [PDF]




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