Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)

Autores
Sivils, Jeffrey C; Storer, Cheryl L.; Galigniana, Mario Daniel; Cox, Marc B.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The large FK506-binding protein FKBP52 has been characterized as an important positive regulator of androgen, glucocorticoid and progesterone receptor signaling pathways. FKBP52 associates with receptor-Hsp90 complexes and is proposed to have roles in both receptor hormone binding and receptor subcellular localization. Data from biochemical and cellular studies have been corroborated in whole animal models as fkbp52-deficient male and female mice display characteristics of androgen, glucocorticoid and/or progesterone insensitivity. FKBP52 receptor specificity and the specific phenotypes displayed by the fkbp52-deficient mice have firmly established FKBP52 as a promising target for the treatment of a variety of hormone-dependent diseases. Recent studies demonstrated that the FKBP52 FK1 domain and the proline-rich loop within this domain are functionally important for FKBP52 regulation of receptor function. Based on these data, efforts are currently underway to target the FKBP52 FK1 domain and the proline-rich loop with small molecule inhibitors.
Fil: Sivils, Jeffrey C. University Of Texas At El Paso; Estados Unidos
Fil: Storer, Cheryl L.. University Of Texas At El Paso; Estados Unidos
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
Fil: Cox, Marc B.. University Of Texas At El Paso; Estados Unidos
Materia
Receptors
Fkbp52
Steroid
Hsp90
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10890

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)Sivils, Jeffrey CStorer, Cheryl L.Galigniana, Mario DanielCox, Marc B.ReceptorsFkbp52SteroidHsp90https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The large FK506-binding protein FKBP52 has been characterized as an important positive regulator of androgen, glucocorticoid and progesterone receptor signaling pathways. FKBP52 associates with receptor-Hsp90 complexes and is proposed to have roles in both receptor hormone binding and receptor subcellular localization. Data from biochemical and cellular studies have been corroborated in whole animal models as fkbp52-deficient male and female mice display characteristics of androgen, glucocorticoid and/or progesterone insensitivity. FKBP52 receptor specificity and the specific phenotypes displayed by the fkbp52-deficient mice have firmly established FKBP52 as a promising target for the treatment of a variety of hormone-dependent diseases. Recent studies demonstrated that the FKBP52 FK1 domain and the proline-rich loop within this domain are functionally important for FKBP52 regulation of receptor function. Based on these data, efforts are currently underway to target the FKBP52 FK1 domain and the proline-rich loop with small molecule inhibitors.Fil: Sivils, Jeffrey C. University Of Texas At El Paso; Estados UnidosFil: Storer, Cheryl L.. University Of Texas At El Paso; Estados UnidosFil: 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; ArgentinaFil: Cox, Marc B.. University Of Texas At El Paso; Estados UnidosElsevier2011-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10890Sivils, Jeffrey C; Storer, Cheryl L.; Galigniana, Mario Daniel; Cox, Marc B.; Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52); Elsevier; Current Opinion In Pharmacology; 11; 4; 8-2011; 314-3191471-48921471-4973enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S147148921100049Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.coph.2011.03.010info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3156321/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:39Zoai:ri.conicet.gov.ar:11336/10890instacron: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 10:11:40.18CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
title Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
spellingShingle Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
Sivils, Jeffrey C
Receptors
Fkbp52
Steroid
Hsp90
title_short Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
title_full Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
title_fullStr Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
title_full_unstemmed Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
title_sort Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
dc.creator.none.fl_str_mv Sivils, Jeffrey C
Storer, Cheryl L.
Galigniana, Mario Daniel
Cox, Marc B.
author Sivils, Jeffrey C
author_facet Sivils, Jeffrey C
Storer, Cheryl L.
Galigniana, Mario Daniel
Cox, Marc B.
author_role author
author2 Storer, Cheryl L.
Galigniana, Mario Daniel
Cox, Marc B.
author2_role author
author
author
dc.subject.none.fl_str_mv Receptors
Fkbp52
Steroid
Hsp90
topic Receptors
Fkbp52
Steroid
Hsp90
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 large FK506-binding protein FKBP52 has been characterized as an important positive regulator of androgen, glucocorticoid and progesterone receptor signaling pathways. FKBP52 associates with receptor-Hsp90 complexes and is proposed to have roles in both receptor hormone binding and receptor subcellular localization. Data from biochemical and cellular studies have been corroborated in whole animal models as fkbp52-deficient male and female mice display characteristics of androgen, glucocorticoid and/or progesterone insensitivity. FKBP52 receptor specificity and the specific phenotypes displayed by the fkbp52-deficient mice have firmly established FKBP52 as a promising target for the treatment of a variety of hormone-dependent diseases. Recent studies demonstrated that the FKBP52 FK1 domain and the proline-rich loop within this domain are functionally important for FKBP52 regulation of receptor function. Based on these data, efforts are currently underway to target the FKBP52 FK1 domain and the proline-rich loop with small molecule inhibitors.
Fil: Sivils, Jeffrey C. University Of Texas At El Paso; Estados Unidos
Fil: Storer, Cheryl L.. University Of Texas At El Paso; Estados Unidos
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
Fil: Cox, Marc B.. University Of Texas At El Paso; Estados Unidos
description The large FK506-binding protein FKBP52 has been characterized as an important positive regulator of androgen, glucocorticoid and progesterone receptor signaling pathways. FKBP52 associates with receptor-Hsp90 complexes and is proposed to have roles in both receptor hormone binding and receptor subcellular localization. Data from biochemical and cellular studies have been corroborated in whole animal models as fkbp52-deficient male and female mice display characteristics of androgen, glucocorticoid and/or progesterone insensitivity. FKBP52 receptor specificity and the specific phenotypes displayed by the fkbp52-deficient mice have firmly established FKBP52 as a promising target for the treatment of a variety of hormone-dependent diseases. Recent studies demonstrated that the FKBP52 FK1 domain and the proline-rich loop within this domain are functionally important for FKBP52 regulation of receptor function. Based on these data, efforts are currently underway to target the FKBP52 FK1 domain and the proline-rich loop with small molecule inhibitors.
publishDate 2011
dc.date.none.fl_str_mv 2011-08
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/11336/10890
Sivils, Jeffrey C; Storer, Cheryl L.; Galigniana, Mario Daniel; Cox, Marc B.; Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52); Elsevier; Current Opinion In Pharmacology; 11; 4; 8-2011; 314-319
1471-4892
1471-4973
url http://hdl.handle.net/11336/10890
identifier_str_mv Sivils, Jeffrey C; Storer, Cheryl L.; Galigniana, Mario Daniel; Cox, Marc B.; Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52); Elsevier; Current Opinion In Pharmacology; 11; 4; 8-2011; 314-319
1471-4892
1471-4973
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/S147148921100049X
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.coph.2011.03.010
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3156321/
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
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