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Papers In Press, published online ahead of print December 26, 2002
CEB, NIDDK/NIH, Bethesda, MD 20892
Corresponding Author: padmam{at}intra.niddk.nih.gov
We expressed green fluorescent proteins (GFP) chimeras of estrogen, retinoic acid, and thyroid hormone receptors (ERs, RARs, and TRs) in HeLa cells to examine nucleo-cytoplasmic 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. Nucleo-cytoplasmic shuttling was demonstrated by hetero-karyon experiments, and energy-dependent blockade of nuclear import. 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 (FRAP) -/+ 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 E2 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.
J. Biol. Chem, 10.1074/jbc.M202752200
Submitted on March 21, 2002
Revised on December 3, 2002
Accepted on December 20, 2002
Dynamic shuttling and intranuclear mobility of nuclear hormone receptors
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