Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β

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Glucocorticoid receptor (GR) is cytoplasmic in the absence of ligand and localizes to the nucleus after steroid binding. Previous evidence demonstrated that the hsp90-based heterocomplex bound to GR is required for the efficient retrotransport of the receptor to the nuclear compartment. We examined...

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Autores principales:	Echeverría, P.C., Mazaira, G., Erlejman, A., Gomez-Sanchez, C., Pilipuk, G.P., Galigniana, M.D.
Formato:	Artículo publishedVersion
Lenguaje:	Inglés
Publicado:	2009
Materias:	digitonin glucocorticoid receptor glycoprotein glycoprotein nup62 heat shock protein 70 heat shock protein 90 karyopherin beta protein Fkbp52 protein p23 protein pp5 radicicol steroid tetratricopeptide repeat protein unclassified drug animal cell article cell membrane permeability controlled study human human cell mouse nonhuman nuclear import nuclear pore nuclear pore complex priority journal protein binding protein cross linking protein expression protein function protein protein interaction structure analysis tetratricopeptide repeat Active Transport, Cell Nucleus Animals beta Karyopherins Cell Line Glycoproteins HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Humans Intramolecular Oxidoreductases Mice Multiprotein Complexes Nuclear Pore Nuclear Pore Complex Proteins Receptors, Glucocorticoid Tacrolimus Binding Proteins
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_02707306_v29_n17_p4788_Echeverria
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	paperaa:paper_02707306_v29_n17_p4788_Echeverria2023-06-12T16:47:17Z Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β Mol. Cell. Biol. 2009;29(17):4788-4797 Echeverría, P.C. Mazaira, G. Erlejman, A. Gomez-Sanchez, C. Pilipuk, G.P. Galigniana, M.D. digitonin glucocorticoid receptor glycoprotein glycoprotein nup62 heat shock protein 70 heat shock protein 90 karyopherin beta protein Fkbp52 protein p23 protein pp5 radicicol steroid tetratricopeptide repeat protein unclassified drug animal cell article cell membrane permeability controlled study human human cell mouse nonhuman nuclear import nuclear pore nuclear pore complex priority journal protein binding protein cross linking protein expression protein function protein protein interaction structure analysis tetratricopeptide repeat Active Transport, Cell Nucleus Animals beta Karyopherins Cell Line Glycoproteins HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Humans Intramolecular Oxidoreductases Mice Multiprotein Complexes Nuclear Pore Nuclear Pore Complex Proteins Receptors, Glucocorticoid Tacrolimus Binding Proteins Glucocorticoid receptor (GR) is cytoplasmic in the absence of ligand and localizes to the nucleus after steroid binding. Previous evidence demonstrated that the hsp90-based heterocomplex bound to GR is required for the efficient retrotransport of the receptor to the nuclear compartment. We examined the putative association of GR and its associated chaperone heterocomplex with structures of the nuclear pore. We found that importin β and the integral nuclear pore glycoprotein Nup62 interact with hsp90, hsp70, p23, and the TPR domain proteins FKBP52 and PP5. Nup62 and GR were able to interact in a more efficient manner when chaperoned by the hsp90-based heterocomplex. Interestingly, the binding of hsp70 and p23 to Nup62 does not require the presence of hsp90, whereas the association of FKBP52 and PP5 is hsp90 dependent, as indicated by the results of experiments where the hsp90 function was disrupted with radicicol. The ability of both FKBP52 and PP5 to interact with Nup62 was abrogated in cells overexpressing the TPR peptide. Importantly, GR cross-linked to the hsp90 heterocomplex was able to translocate to the nucleus in digitonin-permeabilized cells treated with steroid, suggesting that GR could pass through the pore in its untransformed state. Copyright © 2009, American Society for Microbiology. All Rights Reserved. Fil:Echeverría, P.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2009 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_02707306_v29_n17_p4788_Echeverria
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language	Inglés
orig_language_str_mv	eng
topic	digitonin glucocorticoid receptor glycoprotein glycoprotein nup62 heat shock protein 70 heat shock protein 90 karyopherin beta protein Fkbp52 protein p23 protein pp5 radicicol steroid tetratricopeptide repeat protein unclassified drug animal cell article cell membrane permeability controlled study human human cell mouse nonhuman nuclear import nuclear pore nuclear pore complex priority journal protein binding protein cross linking protein expression protein function protein protein interaction structure analysis tetratricopeptide repeat Active Transport, Cell Nucleus Animals beta Karyopherins Cell Line Glycoproteins HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Humans Intramolecular Oxidoreductases Mice Multiprotein Complexes Nuclear Pore Nuclear Pore Complex Proteins Receptors, Glucocorticoid Tacrolimus Binding Proteins
spellingShingle	digitonin glucocorticoid receptor glycoprotein glycoprotein nup62 heat shock protein 70 heat shock protein 90 karyopherin beta protein Fkbp52 protein p23 protein pp5 radicicol steroid tetratricopeptide repeat protein unclassified drug animal cell article cell membrane permeability controlled study human human cell mouse nonhuman nuclear import nuclear pore nuclear pore complex priority journal protein binding protein cross linking protein expression protein function protein protein interaction structure analysis tetratricopeptide repeat Active Transport, Cell Nucleus Animals beta Karyopherins Cell Line Glycoproteins HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Humans Intramolecular Oxidoreductases Mice Multiprotein Complexes Nuclear Pore Nuclear Pore Complex Proteins Receptors, Glucocorticoid Tacrolimus Binding Proteins Echeverría, P.C. Mazaira, G. Erlejman, A. Gomez-Sanchez, C. Pilipuk, G.P. Galigniana, M.D. Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
topic_facet	digitonin glucocorticoid receptor glycoprotein glycoprotein nup62 heat shock protein 70 heat shock protein 90 karyopherin beta protein Fkbp52 protein p23 protein pp5 radicicol steroid tetratricopeptide repeat protein unclassified drug animal cell article cell membrane permeability controlled study human human cell mouse nonhuman nuclear import nuclear pore nuclear pore complex priority journal protein binding protein cross linking protein expression protein function protein protein interaction structure analysis tetratricopeptide repeat Active Transport, Cell Nucleus Animals beta Karyopherins Cell Line Glycoproteins HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Humans Intramolecular Oxidoreductases Mice Multiprotein Complexes Nuclear Pore Nuclear Pore Complex Proteins Receptors, Glucocorticoid Tacrolimus Binding Proteins
description	Glucocorticoid receptor (GR) is cytoplasmic in the absence of ligand and localizes to the nucleus after steroid binding. Previous evidence demonstrated that the hsp90-based heterocomplex bound to GR is required for the efficient retrotransport of the receptor to the nuclear compartment. We examined the putative association of GR and its associated chaperone heterocomplex with structures of the nuclear pore. We found that importin β and the integral nuclear pore glycoprotein Nup62 interact with hsp90, hsp70, p23, and the TPR domain proteins FKBP52 and PP5. Nup62 and GR were able to interact in a more efficient manner when chaperoned by the hsp90-based heterocomplex. Interestingly, the binding of hsp70 and p23 to Nup62 does not require the presence of hsp90, whereas the association of FKBP52 and PP5 is hsp90 dependent, as indicated by the results of experiments where the hsp90 function was disrupted with radicicol. The ability of both FKBP52 and PP5 to interact with Nup62 was abrogated in cells overexpressing the TPR peptide. Importantly, GR cross-linked to the hsp90 heterocomplex was able to translocate to the nucleus in digitonin-permeabilized cells treated with steroid, suggesting that GR could pass through the pore in its untransformed state. Copyright © 2009, American Society for Microbiology. All Rights Reserved.
format	Artículo Artículo publishedVersion
author	Echeverría, P.C. Mazaira, G. Erlejman, A. Gomez-Sanchez, C. Pilipuk, G.P. Galigniana, M.D.
author_facet	Echeverría, P.C. Mazaira, G. Erlejman, A. Gomez-Sanchez, C. Pilipuk, G.P. Galigniana, M.D.
author_sort	Echeverría, P.C.
title	Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
title_short	Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
title_full	Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
title_fullStr	Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
title_full_unstemmed	Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
title_sort	nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with nup62 and importin β
publishDate	2009
url	http://hdl.handle.net/20.500.12110/paper_02707306_v29_n17_p4788_Echeverria
work_keys_str_mv	AT echeverriapc nuclearimportoftheglucocorticoidreceptorhsp90complexthroughthenuclearporecomplexismediatedbyitsinteractionwithnup62andimportinb AT mazairag nuclearimportoftheglucocorticoidreceptorhsp90complexthroughthenuclearporecomplexismediatedbyitsinteractionwithnup62andimportinb AT erlejmana nuclearimportoftheglucocorticoidreceptorhsp90complexthroughthenuclearporecomplexismediatedbyitsinteractionwithnup62andimportinb AT gomezsanchezc nuclearimportoftheglucocorticoidreceptorhsp90complexthroughthenuclearporecomplexismediatedbyitsinteractionwithnup62andimportinb AT pilipukgp nuclearimportoftheglucocorticoidreceptorhsp90complexthroughthenuclearporecomplexismediatedbyitsinteractionwithnup62andimportinb AT galignianamd nuclearimportoftheglucocorticoidreceptorhsp90complexthroughthenuclearporecomplexismediatedbyitsinteractionwithnup62andimportinb
_version_	1769810335225610240

Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β

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