Nucleocytoplasmic trafficking and glucocorticoid receptor function
نویسندگان
چکیده
Robert J.G. Haché, Joanne G.A. Savory and Yvonne A. Lefebvre Departments of Medicine, Biochemistry, Microbiology and Immunology, The Loeb Health Research Institute at the Ottawa Hospital, University of Ottawa, 725 Parkdale Ave., Ottawa, Ontario, Canada, K1Y 4K9 ______________________________________________________________________________________________________ 3 Correspondence: Robert J.G. Haché, Ph.D., Director, Hormones, Growth and Development Program, The Loeb Health Research Institute at the Ottawa Hospital, University of Ottawa, 725 Parkdale Ave., Ottawa, Ontario, Canada, K1Y 4K9. Tel: (613)-798-5555 ext. 6283; Fax: (613)-761-5036; E-mail: [email protected]
منابع مشابه
P-84: Characterization of Androgen Receptor Structure and Nucleocytoplasmic Shuttling of the Rice Field Eel
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Natural mutations of the human glucocorticoid receptor (GR) isoform alpha cause the glucocorticoid resistance syndrome. Mutant receptors may have abnormal interactions with the ligand, target DNA sequences, and/or multiple intracellular proteins, as well as aberrant nucleocytoplasmic trafficking. Using fluorescence recovery after photobleaching (FRAP) analysis, all GR pathologic mutant receptor...
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Glucocorticoid receptor (GR) recycles between an inactive form complexed with heat shock proteins (hsps) and localized to the cytoplasm and a free liganded form that regulates specific gene transcription in the nucleus. We report here that, contrary to previous assumptions, association of GR into hsp-containing complexes is not sufficient to prevent the shuttling or trafficking of the GR across...
متن کاملNuclear export of the glucocorticoid receptor is accelerated by cell fusion-dependent release of calreticulin.
Nucleocytoplasmic exchange of nuclear hormone receptors is hypothesized to allow for rapid and direct interactions with cytoplasmic signaling factors. In addition to recycling between a naïve, chaperone-associated cytoplasmic complex and a liganded chaperone-free nuclear form, the glucocorticoid receptor (GR) has been observed to shuttle between nucleus and cytoplasm. Nuclear export of GR and o...
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The aryl hydrocarbon receptor (AHR) shuttles continuously between cytoplasm and nucleus, unless ligand-binding triggers association with the AHR nuclear translocator (ARNT) and subsequent binding to cognate DNA motifs. We have now identified Val 647 as mandatory residue for export from the nucleus and AHR-function. This residue prevents inactivation of the receptor as a consequence of nuclear s...
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