FKBP51 and FKBP52 in signaling and disease

FKBP51 and FKBP52 are diverse regulators of steroid hormone receptor signaling, including receptor maturation, hormone binding and nuclear translocation. Although structurally similar, they are functionally divergent, which is largely attributed to differences in the FK1 domain and the proline-rich...

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Autores principales:	Storer, C.L., Dickey, C.A., Galigniana, M.D., Rein, T., Cox, M.B.
Formato:	JOUR
Materias:	androgen receptor antineoplastic agent doxorubicin estrogen receptor immunoglobulin enhancer binding protein mineralocorticoid receptor multiprotein complex progesterone receptor protein FKBP51 protein FKBP52 protein kinase B receptor chaperone complex regulator protein steroid hormone steroid receptor tacrolimus unclassified drug Alzheimer disease anxiety disorder bipolar disorder breast carcinogenesis breast tumor cell proliferation cellular distribution complex formation depression disease association drug targeting genital system human immune system immunopathology mental stress metabolic disorder molecular pathology neuropathology nonhuman pathophysiology posttraumatic stress disorder priority journal prostate cancer protein conformation protein folding protein function protein localization protein protein interaction protein structure review schizophrenia signal transduction tauopathy Alzheimer Disease Animals Humans Molecular Chaperones Molecular Targeted Therapy Neoplasms Protein Transport Receptors, Steroid Signal Transduction Stress, Psychological Tacrolimus Binding Proteins
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_10432760_v22_n12_p481_Storer
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_10432760_v22_n12_p481_Storer2023-10-03T15:58:12Z FKBP51 and FKBP52 in signaling and disease Storer, C.L. Dickey, C.A. Galigniana, M.D. Rein, T. Cox, M.B. androgen receptor antineoplastic agent doxorubicin estrogen receptor immunoglobulin enhancer binding protein mineralocorticoid receptor multiprotein complex progesterone receptor protein FKBP51 protein FKBP52 protein kinase B receptor chaperone complex regulator protein steroid hormone steroid receptor tacrolimus unclassified drug Alzheimer disease anxiety disorder bipolar disorder breast carcinogenesis breast tumor cell proliferation cellular distribution complex formation depression disease association drug targeting genital system human immune system immunopathology mental stress metabolic disorder molecular pathology neuropathology nonhuman pathophysiology posttraumatic stress disorder priority journal prostate cancer protein conformation protein folding protein function protein localization protein protein interaction protein structure review schizophrenia signal transduction tauopathy Alzheimer Disease Animals Humans Molecular Chaperones Molecular Targeted Therapy Neoplasms Protein Transport Receptors, Steroid Signal Transduction Stress, Psychological Tacrolimus Binding Proteins FKBP51 and FKBP52 are diverse regulators of steroid hormone receptor signaling, including receptor maturation, hormone binding and nuclear translocation. Although structurally similar, they are functionally divergent, which is largely attributed to differences in the FK1 domain and the proline-rich loop. FKBP51 and FKBP52 have emerged as likely contributors to a variety of hormone-dependent diseases, including stress-related diseases, immune function, reproductive functions and a variety of cancers. In addition, recent studies have implicated FKBP51 and FKBP52 in Alzheimer's disease and other protein aggregation disorders. This review summarizes our current understanding of FKBP51 and FKBP52 interactions within the receptor-chaperone complex, their contributions to health and disease, and their potential as therapeutic targets for the treatment of thesediseases. © 2011 Elsevier Ltd. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_10432760_v22_n12_p481_Storer
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 antineoplastic agent doxorubicin estrogen receptor immunoglobulin enhancer binding protein mineralocorticoid receptor multiprotein complex progesterone receptor protein FKBP51 protein FKBP52 protein kinase B receptor chaperone complex regulator protein steroid hormone steroid receptor tacrolimus unclassified drug Alzheimer disease anxiety disorder bipolar disorder breast carcinogenesis breast tumor cell proliferation cellular distribution complex formation depression disease association drug targeting genital system human immune system immunopathology mental stress metabolic disorder molecular pathology neuropathology nonhuman pathophysiology posttraumatic stress disorder priority journal prostate cancer protein conformation protein folding protein function protein localization protein protein interaction protein structure review schizophrenia signal transduction tauopathy Alzheimer Disease Animals Humans Molecular Chaperones Molecular Targeted Therapy Neoplasms Protein Transport Receptors, Steroid Signal Transduction Stress, Psychological Tacrolimus Binding Proteins
spellingShingle	androgen receptor antineoplastic agent doxorubicin estrogen receptor immunoglobulin enhancer binding protein mineralocorticoid receptor multiprotein complex progesterone receptor protein FKBP51 protein FKBP52 protein kinase B receptor chaperone complex regulator protein steroid hormone steroid receptor tacrolimus unclassified drug Alzheimer disease anxiety disorder bipolar disorder breast carcinogenesis breast tumor cell proliferation cellular distribution complex formation depression disease association drug targeting genital system human immune system immunopathology mental stress metabolic disorder molecular pathology neuropathology nonhuman pathophysiology posttraumatic stress disorder priority journal prostate cancer protein conformation protein folding protein function protein localization protein protein interaction protein structure review schizophrenia signal transduction tauopathy Alzheimer Disease Animals Humans Molecular Chaperones Molecular Targeted Therapy Neoplasms Protein Transport Receptors, Steroid Signal Transduction Stress, Psychological Tacrolimus Binding Proteins Storer, C.L. Dickey, C.A. Galigniana, M.D. Rein, T. Cox, M.B. FKBP51 and FKBP52 in signaling and disease
topic_facet	androgen receptor antineoplastic agent doxorubicin estrogen receptor immunoglobulin enhancer binding protein mineralocorticoid receptor multiprotein complex progesterone receptor protein FKBP51 protein FKBP52 protein kinase B receptor chaperone complex regulator protein steroid hormone steroid receptor tacrolimus unclassified drug Alzheimer disease anxiety disorder bipolar disorder breast carcinogenesis breast tumor cell proliferation cellular distribution complex formation depression disease association drug targeting genital system human immune system immunopathology mental stress metabolic disorder molecular pathology neuropathology nonhuman pathophysiology posttraumatic stress disorder priority journal prostate cancer protein conformation protein folding protein function protein localization protein protein interaction protein structure review schizophrenia signal transduction tauopathy Alzheimer Disease Animals Humans Molecular Chaperones Molecular Targeted Therapy Neoplasms Protein Transport Receptors, Steroid Signal Transduction Stress, Psychological Tacrolimus Binding Proteins
description	FKBP51 and FKBP52 are diverse regulators of steroid hormone receptor signaling, including receptor maturation, hormone binding and nuclear translocation. Although structurally similar, they are functionally divergent, which is largely attributed to differences in the FK1 domain and the proline-rich loop. FKBP51 and FKBP52 have emerged as likely contributors to a variety of hormone-dependent diseases, including stress-related diseases, immune function, reproductive functions and a variety of cancers. In addition, recent studies have implicated FKBP51 and FKBP52 in Alzheimer's disease and other protein aggregation disorders. This review summarizes our current understanding of FKBP51 and FKBP52 interactions within the receptor-chaperone complex, their contributions to health and disease, and their potential as therapeutic targets for the treatment of thesediseases. © 2011 Elsevier Ltd.
format	JOUR
author	Storer, C.L. Dickey, C.A. Galigniana, M.D. Rein, T. Cox, M.B.
author_facet	Storer, C.L. Dickey, C.A. Galigniana, M.D. Rein, T. Cox, M.B.
author_sort	Storer, C.L.
title	FKBP51 and FKBP52 in signaling and disease
title_short	FKBP51 and FKBP52 in signaling and disease
title_full	FKBP51 and FKBP52 in signaling and disease
title_fullStr	FKBP51 and FKBP52 in signaling and disease
title_full_unstemmed	FKBP51 and FKBP52 in signaling and disease
title_sort	fkbp51 and fkbp52 in signaling and disease
url	http://hdl.handle.net/20.500.12110/paper_10432760_v22_n12_p481_Storer
work_keys_str_mv	AT storercl fkbp51andfkbp52insignalinganddisease AT dickeyca fkbp51andfkbp52insignalinganddisease AT galignianamd fkbp51andfkbp52insignalinganddisease AT reint fkbp51andfkbp52insignalinganddisease AT coxmb fkbp51andfkbp52insignalinganddisease
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FKBP51 and FKBP52 in signaling and disease

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