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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/10890
Ver los metadatos del registro completo
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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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score |
13.13397 |