Evidence for glucocorticoid receptor transport on microtubules by dynein
- Autores
- Harrell, Jennifer M.; Murphy, Patrick J.; Morishima, Yoshihiro; Chen, Haifeng; Galigniana, Mario Daniel; Mansfield, John F.; Pratt, William B.
- Año de publicación
- 2004
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Rapid, ligand-dependent movement of glucocorticoid receptors (GR) from cytoplasm to the nucleus is hsp90-dependent, and much of the movement system has been defined. GR.hsp90 heterocomplexes isolated from cells contain one of several hsp90-binding immunophilins that link the complex to cytoplasmic dynein, a molecular motor that processes along microtubular tracks to the nucleus. The immunophilins link to dynein indirectly via the dynamitin component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Although it is known that rapid, hsp90-dependent GR movement requires intact microtubules, it has not been shown that the movement is dynein-dependent. Here, we show that overexpression of dynamitin, which blocks movement by dissociating the dynein motor from its cargo, inhibits ligand-dependent movement of the GR to the nucleus. We show that native GR.hsp90.immnunophilin complexes contain dynamitin as well as dynein and that GR heterocomplexes isolated from cytosol containing paclitaxel and GTP to stabilize microtubules also contain tubulin. The complete movement system, including the dynein motor complex and tubulin, can be assembled under cell-free conditions by incubating GR immune pellets with paclitaxel/GTP-stabilized cytosol prepared from GR(-) L cells. This is the first evidence that the movement of a steroid receptor is dynein-dependent, and it is the first isolation of a steroid receptor bound to the entire system that determines its retrograde movement.
Fil: Harrell, Jennifer M.. University of Michigan; Estados Unidos
Fil: Murphy, Patrick J.. University of Michigan; Estados Unidos
Fil: Morishima, Yoshihiro. University of Michigan; Estados Unidos
Fil: Chen, Haifeng. University of Michigan; Estados Unidos
Fil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Mansfield, John F.. University of Michigan; Estados Unidos
Fil: Pratt, William B.. University of Michigan; Estados Unidos - Materia
-
Cell Nucleus
Hsp 90
Immunophilins
Microtubules-Associated Proteins - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/29104
Ver los metadatos del registro completo
id |
CONICETDig_308565c2d75d7c978623b68a92b92e48 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/29104 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Evidence for glucocorticoid receptor transport on microtubules by dyneinHarrell, Jennifer M.Murphy, Patrick J.Morishima, YoshihiroChen, HaifengGaligniana, Mario DanielMansfield, John F.Pratt, William B.Cell NucleusHsp 90ImmunophilinsMicrotubules-Associated Proteinshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Rapid, ligand-dependent movement of glucocorticoid receptors (GR) from cytoplasm to the nucleus is hsp90-dependent, and much of the movement system has been defined. GR.hsp90 heterocomplexes isolated from cells contain one of several hsp90-binding immunophilins that link the complex to cytoplasmic dynein, a molecular motor that processes along microtubular tracks to the nucleus. The immunophilins link to dynein indirectly via the dynamitin component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Although it is known that rapid, hsp90-dependent GR movement requires intact microtubules, it has not been shown that the movement is dynein-dependent. Here, we show that overexpression of dynamitin, which blocks movement by dissociating the dynein motor from its cargo, inhibits ligand-dependent movement of the GR to the nucleus. We show that native GR.hsp90.immnunophilin complexes contain dynamitin as well as dynein and that GR heterocomplexes isolated from cytosol containing paclitaxel and GTP to stabilize microtubules also contain tubulin. The complete movement system, including the dynein motor complex and tubulin, can be assembled under cell-free conditions by incubating GR immune pellets with paclitaxel/GTP-stabilized cytosol prepared from GR(-) L cells. This is the first evidence that the movement of a steroid receptor is dynein-dependent, and it is the first isolation of a steroid receptor bound to the entire system that determines its retrograde movement.Fil: Harrell, Jennifer M.. University of Michigan; Estados UnidosFil: Murphy, Patrick J.. University of Michigan; Estados UnidosFil: Morishima, Yoshihiro. University of Michigan; Estados UnidosFil: Chen, Haifeng. University of Michigan; Estados UnidosFil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Mansfield, John F.. University of Michigan; Estados UnidosFil: Pratt, William B.. University of Michigan; Estados UnidosAmerican Society for Biochemistry and Molecular Biology2004info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/29104Harrell, Jennifer M.; Murphy, Patrick J.; Morishima, Yoshihiro; Chen, Haifeng; Galigniana, Mario Daniel; et al.; Evidence for glucocorticoid receptor transport on microtubules by dynein; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 52; 2004; 54647-546540021-92581083-351XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/279/52/54647.longinfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M406863200info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:09:25Zoai:ri.conicet.gov.ar:11336/29104instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 12:09:25.502CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Evidence for glucocorticoid receptor transport on microtubules by dynein |
title |
Evidence for glucocorticoid receptor transport on microtubules by dynein |
spellingShingle |
Evidence for glucocorticoid receptor transport on microtubules by dynein Harrell, Jennifer M. Cell Nucleus Hsp 90 Immunophilins Microtubules-Associated Proteins |
title_short |
Evidence for glucocorticoid receptor transport on microtubules by dynein |
title_full |
Evidence for glucocorticoid receptor transport on microtubules by dynein |
title_fullStr |
Evidence for glucocorticoid receptor transport on microtubules by dynein |
title_full_unstemmed |
Evidence for glucocorticoid receptor transport on microtubules by dynein |
title_sort |
Evidence for glucocorticoid receptor transport on microtubules by dynein |
dc.creator.none.fl_str_mv |
Harrell, Jennifer M. Murphy, Patrick J. Morishima, Yoshihiro Chen, Haifeng Galigniana, Mario Daniel Mansfield, John F. Pratt, William B. |
author |
Harrell, Jennifer M. |
author_facet |
Harrell, Jennifer M. Murphy, Patrick J. Morishima, Yoshihiro Chen, Haifeng Galigniana, Mario Daniel Mansfield, John F. Pratt, William B. |
author_role |
author |
author2 |
Murphy, Patrick J. Morishima, Yoshihiro Chen, Haifeng Galigniana, Mario Daniel Mansfield, John F. Pratt, William B. |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
Cell Nucleus Hsp 90 Immunophilins Microtubules-Associated Proteins |
topic |
Cell Nucleus Hsp 90 Immunophilins Microtubules-Associated Proteins |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Rapid, ligand-dependent movement of glucocorticoid receptors (GR) from cytoplasm to the nucleus is hsp90-dependent, and much of the movement system has been defined. GR.hsp90 heterocomplexes isolated from cells contain one of several hsp90-binding immunophilins that link the complex to cytoplasmic dynein, a molecular motor that processes along microtubular tracks to the nucleus. The immunophilins link to dynein indirectly via the dynamitin component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Although it is known that rapid, hsp90-dependent GR movement requires intact microtubules, it has not been shown that the movement is dynein-dependent. Here, we show that overexpression of dynamitin, which blocks movement by dissociating the dynein motor from its cargo, inhibits ligand-dependent movement of the GR to the nucleus. We show that native GR.hsp90.immnunophilin complexes contain dynamitin as well as dynein and that GR heterocomplexes isolated from cytosol containing paclitaxel and GTP to stabilize microtubules also contain tubulin. The complete movement system, including the dynein motor complex and tubulin, can be assembled under cell-free conditions by incubating GR immune pellets with paclitaxel/GTP-stabilized cytosol prepared from GR(-) L cells. This is the first evidence that the movement of a steroid receptor is dynein-dependent, and it is the first isolation of a steroid receptor bound to the entire system that determines its retrograde movement. Fil: Harrell, Jennifer M.. University of Michigan; Estados Unidos Fil: Murphy, Patrick J.. University of Michigan; Estados Unidos Fil: Morishima, Yoshihiro. University of Michigan; Estados Unidos Fil: Chen, Haifeng. University of Michigan; Estados Unidos Fil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina Fil: Mansfield, John F.. University of Michigan; Estados Unidos Fil: Pratt, William B.. University of Michigan; Estados Unidos |
description |
Rapid, ligand-dependent movement of glucocorticoid receptors (GR) from cytoplasm to the nucleus is hsp90-dependent, and much of the movement system has been defined. GR.hsp90 heterocomplexes isolated from cells contain one of several hsp90-binding immunophilins that link the complex to cytoplasmic dynein, a molecular motor that processes along microtubular tracks to the nucleus. The immunophilins link to dynein indirectly via the dynamitin component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Although it is known that rapid, hsp90-dependent GR movement requires intact microtubules, it has not been shown that the movement is dynein-dependent. Here, we show that overexpression of dynamitin, which blocks movement by dissociating the dynein motor from its cargo, inhibits ligand-dependent movement of the GR to the nucleus. We show that native GR.hsp90.immnunophilin complexes contain dynamitin as well as dynein and that GR heterocomplexes isolated from cytosol containing paclitaxel and GTP to stabilize microtubules also contain tubulin. The complete movement system, including the dynein motor complex and tubulin, can be assembled under cell-free conditions by incubating GR immune pellets with paclitaxel/GTP-stabilized cytosol prepared from GR(-) L cells. This is the first evidence that the movement of a steroid receptor is dynein-dependent, and it is the first isolation of a steroid receptor bound to the entire system that determines its retrograde movement. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/29104 Harrell, Jennifer M.; Murphy, Patrick J.; Morishima, Yoshihiro; Chen, Haifeng; Galigniana, Mario Daniel; et al.; Evidence for glucocorticoid receptor transport on microtubules by dynein; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 52; 2004; 54647-54654 0021-9258 1083-351X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/29104 |
identifier_str_mv |
Harrell, Jennifer M.; Murphy, Patrick J.; Morishima, Yoshihiro; Chen, Haifeng; Galigniana, Mario Daniel; et al.; Evidence for glucocorticoid receptor transport on microtubules by dynein; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 52; 2004; 54647-54654 0021-9258 1083-351X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/279/52/54647.long info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M406863200 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
_version_ |
1846782472023441408 |
score |
12.982451 |