Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
- Autores
- Pratt, William B.; Galigniana, Mario Daniel; Harrell, Jennifer M.; de Franco, Donald B.
- Año de publicación
- 2004
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytoplasm and the nucleus. In the case of signalling proteins that act as transcription factors, the client protein.hsp90 complexes also contain one of several TPR domain immunophilins or immunophilin homologs that bind to a TPR domain binding site on hsp90. Using several intracellular receptors and the tumor suppressor p53 as examples, we review evidence that dynamic assembly of heterocomplexes with hsp90 is required for rapid movement through the cytoplasm to the nucleus along microtubular tracks. The role of the immunophilin in this system is to connect the client protein.hsp90 complex to cytoplasmic dynein, the motor protein for retrograde movement toward the nucleus. Upon arrival at the nuclear pores, the receptor.hsp90.immunophilin complexes are transferred to the nuclear interior by importin-dependent facilitated diffusion. The unliganded receptors then distribute within the nucleus to diffuse patches from which they proceed in a ligand-dependent manner to discrete nuclear foci where chromatin binding occurs. We review evidence that dynamic assembly of heterocomplexes with hsp90 is required for movement to these foci and for the dynamic exchange of transcription factors between chromatin and the nucleoplasm.
Fil: Pratt, William B.. University of Michigan; Estados Unidos
Fil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Harrell, Jennifer M.. University of Michigan; Estados Unidos
Fil: de Franco, Donald B.. University of Pittsburgh; Estados Unidos - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/29102
Ver los metadatos del registro completo
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Role of hsp90 and the hsp90-binding immunophilins in signalling protein movementPratt, William B.Galigniana, Mario DanielHarrell, Jennifer M.de Franco, Donald B.https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytoplasm and the nucleus. In the case of signalling proteins that act as transcription factors, the client protein.hsp90 complexes also contain one of several TPR domain immunophilins or immunophilin homologs that bind to a TPR domain binding site on hsp90. Using several intracellular receptors and the tumor suppressor p53 as examples, we review evidence that dynamic assembly of heterocomplexes with hsp90 is required for rapid movement through the cytoplasm to the nucleus along microtubular tracks. The role of the immunophilin in this system is to connect the client protein.hsp90 complex to cytoplasmic dynein, the motor protein for retrograde movement toward the nucleus. Upon arrival at the nuclear pores, the receptor.hsp90.immunophilin complexes are transferred to the nuclear interior by importin-dependent facilitated diffusion. The unliganded receptors then distribute within the nucleus to diffuse patches from which they proceed in a ligand-dependent manner to discrete nuclear foci where chromatin binding occurs. We review evidence that dynamic assembly of heterocomplexes with hsp90 is required for movement to these foci and for the dynamic exchange of transcription factors between chromatin and the nucleoplasm.Fil: Pratt, William B.. University of Michigan; Estados UnidosFil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Harrell, Jennifer M.. University of Michigan; Estados UnidosFil: de Franco, Donald B.. University of Pittsburgh; Estados UnidosElsevier Inc2004info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/29102Pratt, William B.; Galigniana, Mario Daniel; Harrell, Jennifer M.; de Franco, Donald B.; Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement; Elsevier Inc; Cellular Signalling; 16; 8; -1-2004; 857-8720898-65681873-3913CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0898656804000257?via%3Dihubinfo:eu-repo/semantics/altIdentifier/url/10.1016/j.cellsig.2004.02.004info:eu-repo/semantics/altIdentifier/pmid/15157665info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:48:50Zoai:ri.conicet.gov.ar:11336/29102instacron: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:34982025-09-29 09:48:50.484CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement |
title |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement |
spellingShingle |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement Pratt, William B. |
title_short |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement |
title_full |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement |
title_fullStr |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement |
title_full_unstemmed |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement |
title_sort |
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement |
dc.creator.none.fl_str_mv |
Pratt, William B. Galigniana, Mario Daniel Harrell, Jennifer M. de Franco, Donald B. |
author |
Pratt, William B. |
author_facet |
Pratt, William B. Galigniana, Mario Daniel Harrell, Jennifer M. de Franco, Donald B. |
author_role |
author |
author2 |
Galigniana, Mario Daniel Harrell, Jennifer M. de Franco, Donald B. |
author2_role |
author author author |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytoplasm and the nucleus. In the case of signalling proteins that act as transcription factors, the client protein.hsp90 complexes also contain one of several TPR domain immunophilins or immunophilin homologs that bind to a TPR domain binding site on hsp90. Using several intracellular receptors and the tumor suppressor p53 as examples, we review evidence that dynamic assembly of heterocomplexes with hsp90 is required for rapid movement through the cytoplasm to the nucleus along microtubular tracks. The role of the immunophilin in this system is to connect the client protein.hsp90 complex to cytoplasmic dynein, the motor protein for retrograde movement toward the nucleus. Upon arrival at the nuclear pores, the receptor.hsp90.immunophilin complexes are transferred to the nuclear interior by importin-dependent facilitated diffusion. The unliganded receptors then distribute within the nucleus to diffuse patches from which they proceed in a ligand-dependent manner to discrete nuclear foci where chromatin binding occurs. We review evidence that dynamic assembly of heterocomplexes with hsp90 is required for movement to these foci and for the dynamic exchange of transcription factors between chromatin and the nucleoplasm. Fil: Pratt, William B.. University of Michigan; Estados Unidos Fil: Galigniana, Mario Daniel. University of Michigan; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Harrell, Jennifer M.. University of Michigan; Estados Unidos Fil: de Franco, Donald B.. University of Pittsburgh; Estados Unidos |
description |
The ubiquitous protein chaperone hsp90 has been shown to regulate more than 100 proteins involved in cellular signalling. These proteins are called 'client proteins' for hsp90, and a multiprotein hsp90/hsp70-based chaperone machinery forms client protein.hsp90 heterocomplexes in the cytoplasm and the nucleus. In the case of signalling proteins that act as transcription factors, the client protein.hsp90 complexes also contain one of several TPR domain immunophilins or immunophilin homologs that bind to a TPR domain binding site on hsp90. Using several intracellular receptors and the tumor suppressor p53 as examples, we review evidence that dynamic assembly of heterocomplexes with hsp90 is required for rapid movement through the cytoplasm to the nucleus along microtubular tracks. The role of the immunophilin in this system is to connect the client protein.hsp90 complex to cytoplasmic dynein, the motor protein for retrograde movement toward the nucleus. Upon arrival at the nuclear pores, the receptor.hsp90.immunophilin complexes are transferred to the nuclear interior by importin-dependent facilitated diffusion. The unliganded receptors then distribute within the nucleus to diffuse patches from which they proceed in a ligand-dependent manner to discrete nuclear foci where chromatin binding occurs. We review evidence that dynamic assembly of heterocomplexes with hsp90 is required for movement to these foci and for the dynamic exchange of transcription factors between chromatin and the nucleoplasm. |
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/11336/29102 Pratt, William B.; Galigniana, Mario Daniel; Harrell, Jennifer M.; de Franco, Donald B.; Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement; Elsevier Inc; Cellular Signalling; 16; 8; -1-2004; 857-872 0898-6568 1873-3913 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/29102 |
identifier_str_mv |
Pratt, William B.; Galigniana, Mario Daniel; Harrell, Jennifer M.; de Franco, Donald B.; Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement; Elsevier Inc; Cellular Signalling; 16; 8; -1-2004; 857-872 0898-6568 1873-3913 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.sciencedirect.com/science/article/pii/S0898656804000257?via%3Dihub info:eu-repo/semantics/altIdentifier/url/10.1016/j.cellsig.2004.02.004 info:eu-repo/semantics/altIdentifier/pmid/15157665 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Inc |
publisher.none.fl_str_mv |
Elsevier Inc |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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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 |
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1844613514877992960 |
score |
13.070432 |