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Vol. 10, Issue 2, 471-486, February 1999
Reveals a
Role for Ligand in the Nuclear Distribution of the Receptor
§
*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 
(ER ) 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.
These authors contributed equally to this work.
Corresponding author. E-mail address:
hagerg{at}exchange.nih.gov.
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.
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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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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. [Abstract] [Full Text]
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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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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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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. [Abstract] [Full Text]
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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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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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 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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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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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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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. [Abstract] [PDF]
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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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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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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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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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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.-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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