Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
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 subce...
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2011
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14714892_v11_n4_p314_Sivils http://hdl.handle.net/20.500.12110/paper_14714892_v11_n4_p314_Sivils |
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paper:paper_14714892_v11_n4_p314_Sivils2023-06-08T16:17:21Z Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52) androgen receptor dynein adenosine triphosphatase estrogen receptor fk 506 binding protein fk 506 binding protein 52 geldanamycin glucocorticoid receptor heat shock protein 90 karyopherin alpha karyopherin beta peptidylprolyl isomerase progesterone receptor steroid receptor tacrolimus unclassified drug article breast tumor cellular distribution complex formation cytoplasm endometriosis female infertility hormone binding human nonhuman nuclear localization signal nuclear pore complex oxidative stress priority journal prostate cancer protein degradation protein phosphorylation protein protein interaction Animals Drug Delivery Systems Drug Design Female Humans Male Mice Receptors, Androgen Receptors, Glucocorticoid Receptors, Progesterone Signal Transduction Tacrolimus Binding Proteins 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. © 2011 Elsevier Ltd. All rights reserved. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14714892_v11_n4_p314_Sivils http://hdl.handle.net/20.500.12110/paper_14714892_v11_n4_p314_Sivils |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
androgen receptor dynein adenosine triphosphatase estrogen receptor fk 506 binding protein fk 506 binding protein 52 geldanamycin glucocorticoid receptor heat shock protein 90 karyopherin alpha karyopherin beta peptidylprolyl isomerase progesterone receptor steroid receptor tacrolimus unclassified drug article breast tumor cellular distribution complex formation cytoplasm endometriosis female infertility hormone binding human nonhuman nuclear localization signal nuclear pore complex oxidative stress priority journal prostate cancer protein degradation protein phosphorylation protein protein interaction Animals Drug Delivery Systems Drug Design Female Humans Male Mice Receptors, Androgen Receptors, Glucocorticoid Receptors, Progesterone Signal Transduction Tacrolimus Binding Proteins |
| spellingShingle |
androgen receptor dynein adenosine triphosphatase estrogen receptor fk 506 binding protein fk 506 binding protein 52 geldanamycin glucocorticoid receptor heat shock protein 90 karyopherin alpha karyopherin beta peptidylprolyl isomerase progesterone receptor steroid receptor tacrolimus unclassified drug article breast tumor cellular distribution complex formation cytoplasm endometriosis female infertility hormone binding human nonhuman nuclear localization signal nuclear pore complex oxidative stress priority journal prostate cancer protein degradation protein phosphorylation protein protein interaction Animals Drug Delivery Systems Drug Design Female Humans Male Mice Receptors, Androgen Receptors, Glucocorticoid Receptors, Progesterone Signal Transduction Tacrolimus Binding Proteins Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52) |
| topic_facet |
androgen receptor dynein adenosine triphosphatase estrogen receptor fk 506 binding protein fk 506 binding protein 52 geldanamycin glucocorticoid receptor heat shock protein 90 karyopherin alpha karyopherin beta peptidylprolyl isomerase progesterone receptor steroid receptor tacrolimus unclassified drug article breast tumor cellular distribution complex formation cytoplasm endometriosis female infertility hormone binding human nonhuman nuclear localization signal nuclear pore complex oxidative stress priority journal prostate cancer protein degradation protein phosphorylation protein protein interaction Animals Drug Delivery Systems Drug Design Female Humans Male Mice Receptors, Androgen Receptors, Glucocorticoid Receptors, Progesterone Signal Transduction Tacrolimus Binding Proteins |
| 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. © 2011 Elsevier Ltd. All rights reserved. |
| title |
Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52) |
| 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) |
| publishDate |
2011 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14714892_v11_n4_p314_Sivils http://hdl.handle.net/20.500.12110/paper_14714892_v11_n4_p314_Sivils |
| _version_ |
1768544289318502400 |