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J. Biol. Chem., Vol. 278, Issue 14, 12425-12432, April 4, 2003
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,¶
From the We expressed green fluorescent protein
(GFP) chimeras of estrogen, retinoic acid, and thyroid hormone
receptors (ERs, RARs, and TRs, respectively) in HeLa cells to examine
nucleocytoplasmic shuttling and intranuclear mobility of nuclear
hormone receptors (NRs) by confocal microscopy. These receptors were
predominantly in the nucleus and, interestingly, underwent
intranuclear reorganization after ligand treatment.
Nucleocytoplasmic shuttling was demonstrated by
heterokaryon experiments and energy-dependent
blockade of nuclear import and leptomycin-dependent
blockade of nuclear export. Ligand addition decreased shuttling by
GFP-ER, whereas heterodimerization with retinoid X receptor helped
maintain TR and RAR within the nucleus. Intranuclear mobility of the
GFP-NRs was studied by fluorescence recovery after
photo-bleaching ± cognate ligands. Both GFP-TR and GFP-RAR
moved rapidly in the nucleus, and ligand binding did not significantly
affect their mobility. In contrast, estrogen binding decreased the
mobility of GFP-ER and also increased the fraction of GFP-ER that was
unable to diffuse. These effects were even more pronounced with
tamoxifen. Co-transfection of the co-activator, SRC-1, further
slowed the mobility of liganded GFP-ER. Our findings suggest estradiol
and tamoxifen exert differential effects on the intranuclear mobility
of GFP-ER. They also show that ligand-binding and
protein-protein interactions can affect the intracellular mobility of
some NRs and thereby may contribute to their biological activity.
Molecular Regulation and Neuroendocrinology
Section, Clinical Endocrinology Branch, NIDDK and
§ Laboratory of Receptor Biology and Gene Expression, NCI,
National Institutes of Health, Bethesda, Maryland 20892
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