Molecular chaperones shape steroid receptor action and pharmacologic strategies

Autores
Mazaira, Gisela Ileana; Lagadari, Mariana; Elerjman, Alejandra G.; Galigniana, Mario Daniel
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Chaperone oligomers exist in cell cytosols as preassembled heterocomplexes that function as protein-folding molecular machines able to assemble essential proteins related to families that embrace steroid receptors, protein-kinases, ubiquitin-ligases, and transcription factors, among other families of key proteins. Actually, steroid receptors may be considered a particular subset of transcription factors that can be activated by specific ligands. Some of them are primarily located in the cytoplasm, others are constitutively nuclear, but regardless of their subcellular distribution, they are constantly shuttling between both compartments in a highly dynamic manner. The chaperone heterocomplex associated to steroid receptors is not only involved in the stabilization of their conformation preventing their degradation by the proteasome, but it is also critical for the molecular mechanism of transport of these receptors and their subnuclear redistribution. In this article we summarized some of the general properties of molecular chaperones, in particular those belonging to a subfamily that is highly inducible by thermal shock, the heat-shock proteins, and review the most recent findings performed in the field of soluble protein trafficking, where molecular chaperones play a critical role.
Fil: Mazaira, Gisela Ileana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Lagadari, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Elerjman, Alejandra G.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Materia
STEROID RECEPTOR
HSP90
IMMUNOPHILINS
FKBP52
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/4125
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Molecular chaperones shape steroid receptor action and pharmacologic strategiesMazaira, Gisela IleanaLagadari, MarianaElerjman, Alejandra G.Galigniana, Mario DanielSTEROID RECEPTORHSP90IMMUNOPHILINSFKBP52https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Chaperone oligomers exist in cell cytosols as preassembled heterocomplexes that function as protein-folding molecular machines able to assemble essential proteins related to families that embrace steroid receptors, protein-kinases, ubiquitin-ligases, and transcription factors, among other families of key proteins. Actually, steroid receptors may be considered a particular subset of transcription factors that can be activated by specific ligands. Some of them are primarily located in the cytoplasm, others are constitutively nuclear, but regardless of their subcellular distribution, they are constantly shuttling between both compartments in a highly dynamic manner. The chaperone heterocomplex associated to steroid receptors is not only involved in the stabilization of their conformation preventing their degradation by the proteasome, but it is also critical for the molecular mechanism of transport of these receptors and their subnuclear redistribution. In this article we summarized some of the general properties of molecular chaperones, in particular those belonging to a subfamily that is highly inducible by thermal shock, the heat-shock proteins, and review the most recent findings performed in the field of soluble protein trafficking, where molecular chaperones play a critical role.Fil: Mazaira, Gisela Ileana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Lagadari, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); ArgentinaFil: Elerjman, Alejandra G.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaJacobs Publisher2015-03-31info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4125Mazaira, Gisela Ileana; Lagadari, Mariana; Elerjman, Alejandra G.; Galigniana, Mario Daniel; Molecular chaperones shape steroid receptor action and pharmacologic strategies; Jacobs Publisher; Jacobs Journal of Cell and Molecular Biology; 1; 1; 31-3-2015; 1-41306-09612381-2761enginfo:eu-repo/semantics/altIdentifier/url/http://www.jacobspublishers.com/index.php/j-j-cell-mol-bio-1-1-004info:eu-repo/semantics/altIdentifier/issn/1306-0961info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:20Zoai:ri.conicet.gov.ar:11336/4125instacron: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:34982025-09-03 09:44:20.885CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Molecular chaperones shape steroid receptor action and pharmacologic strategies
title Molecular chaperones shape steroid receptor action and pharmacologic strategies
spellingShingle Molecular chaperones shape steroid receptor action and pharmacologic strategies
Mazaira, Gisela Ileana
STEROID RECEPTOR
HSP90
IMMUNOPHILINS
FKBP52
title_short Molecular chaperones shape steroid receptor action and pharmacologic strategies
title_full Molecular chaperones shape steroid receptor action and pharmacologic strategies
title_fullStr Molecular chaperones shape steroid receptor action and pharmacologic strategies
title_full_unstemmed Molecular chaperones shape steroid receptor action and pharmacologic strategies
title_sort Molecular chaperones shape steroid receptor action and pharmacologic strategies
dc.creator.none.fl_str_mv Mazaira, Gisela Ileana
Lagadari, Mariana
Elerjman, Alejandra G.
Galigniana, Mario Daniel
author Mazaira, Gisela Ileana
author_facet Mazaira, Gisela Ileana
Lagadari, Mariana
Elerjman, Alejandra G.
Galigniana, Mario Daniel
author_role author
author2 Lagadari, Mariana
Elerjman, Alejandra G.
Galigniana, Mario Daniel
author2_role author
author
author
dc.subject.none.fl_str_mv STEROID RECEPTOR
HSP90
IMMUNOPHILINS
FKBP52
topic STEROID RECEPTOR
HSP90
IMMUNOPHILINS
FKBP52
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Chaperone oligomers exist in cell cytosols as preassembled heterocomplexes that function as protein-folding molecular machines able to assemble essential proteins related to families that embrace steroid receptors, protein-kinases, ubiquitin-ligases, and transcription factors, among other families of key proteins. Actually, steroid receptors may be considered a particular subset of transcription factors that can be activated by specific ligands. Some of them are primarily located in the cytoplasm, others are constitutively nuclear, but regardless of their subcellular distribution, they are constantly shuttling between both compartments in a highly dynamic manner. The chaperone heterocomplex associated to steroid receptors is not only involved in the stabilization of their conformation preventing their degradation by the proteasome, but it is also critical for the molecular mechanism of transport of these receptors and their subnuclear redistribution. In this article we summarized some of the general properties of molecular chaperones, in particular those belonging to a subfamily that is highly inducible by thermal shock, the heat-shock proteins, and review the most recent findings performed in the field of soluble protein trafficking, where molecular chaperones play a critical role.
Fil: Mazaira, Gisela Ileana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Lagadari, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Elerjman, Alejandra G.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Galigniana, Mario Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
description Chaperone oligomers exist in cell cytosols as preassembled heterocomplexes that function as protein-folding molecular machines able to assemble essential proteins related to families that embrace steroid receptors, protein-kinases, ubiquitin-ligases, and transcription factors, among other families of key proteins. Actually, steroid receptors may be considered a particular subset of transcription factors that can be activated by specific ligands. Some of them are primarily located in the cytoplasm, others are constitutively nuclear, but regardless of their subcellular distribution, they are constantly shuttling between both compartments in a highly dynamic manner. The chaperone heterocomplex associated to steroid receptors is not only involved in the stabilization of their conformation preventing their degradation by the proteasome, but it is also critical for the molecular mechanism of transport of these receptors and their subnuclear redistribution. In this article we summarized some of the general properties of molecular chaperones, in particular those belonging to a subfamily that is highly inducible by thermal shock, the heat-shock proteins, and review the most recent findings performed in the field of soluble protein trafficking, where molecular chaperones play a critical role.
publishDate 2015
dc.date.none.fl_str_mv 2015-03-31
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/11336/4125
Mazaira, Gisela Ileana; Lagadari, Mariana; Elerjman, Alejandra G.; Galigniana, Mario Daniel; Molecular chaperones shape steroid receptor action and pharmacologic strategies; Jacobs Publisher; Jacobs Journal of Cell and Molecular Biology; 1; 1; 31-3-2015; 1-4
1306-0961
2381-2761
url http://hdl.handle.net/11336/4125
identifier_str_mv Mazaira, Gisela Ileana; Lagadari, Mariana; Elerjman, Alejandra G.; Galigniana, Mario Daniel; Molecular chaperones shape steroid receptor action and pharmacologic strategies; Jacobs Publisher; Jacobs Journal of Cell and Molecular Biology; 1; 1; 31-3-2015; 1-4
1306-0961
2381-2761
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jacobspublishers.com/index.php/j-j-cell-mol-bio-1-1-004
info:eu-repo/semantics/altIdentifier/issn/1306-0961
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Jacobs Publisher
publisher.none.fl_str_mv Jacobs Publisher
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_ 1842268659779633152
score 13.13397

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