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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2011
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| LEADER | 28950caa a22024377a 4500 | ||
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| 001 | PAPER-10091 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230607131855.0 | ||
| 008 | 190411s2011 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-82555167019 | |
| 024 | 7 | |2 cas |a doxorubicin, 23214-92-8, 25316-40-9; protein kinase B, 148640-14-6; tacrolimus, 104987-11-3; Molecular Chaperones; Receptors, Steroid; Tacrolimus Binding Proteins, 5.2.1.-; tacrolimus binding protein 4, 5.2.1.-; tacrolimus binding protein 5, 5.2.1.8 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a TENME | ||
| 100 | 1 | |a Storer, C.L. | |
| 245 | 1 | 0 | |a FKBP51 and FKBP52 in signaling and disease |
| 260 | |c 2011 | ||
| 270 | 1 | 0 | |m Cox, M.B.; The Border Biomedical Research Center and Department of Biological Sciences, University of Texas at El Paso, El Paso, TX 79968, United States; email: mbcox@utep.edu |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a 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. |l eng | |
| 536 | |a Detalles de la financiación: National Institute on Aging | ||
| 536 | |a Detalles de la financiación: National Institutes of Health, SC1GM084863 | ||
| 536 | |a Detalles de la financiación: Secretaría de Ciencia y Técnica, Universidad de Buenos Aires, R01NS073899, R00AG031291, X085 | ||
| 536 | |a Detalles de la financiación: Texas A and M University-Central Texas | ||
| 536 | |a Detalles de la financiación: National Center for Research Resources, NCRR | ||
| 536 | |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, PICT2011-1170 | ||
| 536 | |a Detalles de la financiación: National Institute of General Medical Sciences | ||
| 536 | |a Detalles de la financiación: National Institute of Neurological Disorders and Stroke | ||
| 536 | |a Detalles de la financiación: The authors are supported in part by Grant 5G12RR008124 [to the Border Biomedical Research Center (BBRC)/University of Texas at El Paso] from the National Center for Research Resources (NCRR), a component of the National Institutes of Health (NIH). The contents of this article are solely the responsibility of the authors and do not necessarily represent the official views of NCRR or NIH. We thank the BBRC Biomolecule Analysis Core Facility (BACF), Tissue Culture Core Facility (TCF), and the DNA Analysis Core Facility (DACF) for use of instruments. M.B.C. is also supported in part by American Recovery and Reinvestment Act (ARRA) funds through Grant SC1GM084863 from the National Institute of General Medical Sciences, NIH. M.D.G. is supported by grants ANPCyT (PICT2011-1170) and UBACyT (X085). C.A.D. is supported by grants R01NS073899 and R00AG031291 from the National Institute of Neurological Disorders and Stroke and the National Institute on Aging, respectively. AKT serine/threonine protein kinase that regulates apoptosis, cell migration, transcription, proliferation and glucose metabolism. Antineoplastic therapy chemotherapy that targets all actively dividing cells. β-Importin during nuclear import, β-importin tethers incoming proteins to the nuclear pore complex. FKBP51 51-kDa FK506 binding protein that binds the immunosuppressive drug FK506 without initiating immunosuppression. FKBP52 52-kDa FK506 binding protein that binds the immunosppressive drug FK506 without initiating immunosuppression. FK1 domain FKBP12-like domain 1 of FKBP51 and FKPB52, responsible for binding to FK506, for PPIase activity and for steroid hormone receptor regulation. FK2 domain FKBP12-like domain 2, present in FKBP51 and FKBP52; differs slightly from the FK1 and lacks PPIase and FK506 binding ability. FK506 also called tacrolimus, a macrolide drug that complexes with FKBP12 and inhibits calcineurin phosphatase activity. This leads to immunosuppression by blocking T-cell signal transduction cascades and interleukin-2 transcription. Geldanamycin benzoquinone ansamycin antibiotic that directly binds HSP90 and inhibits its function. HSP90 the 90-kDa heat shock protein is a molecular chaperone involved in protein folding, tumor repression and cell signaling. Steroid hormone receptors require association with HSP90 to fold to a conformation capable of binding to a ligand. Hypothalamus pituitary adrenal (HPA) axis interactions between the hypothalamus, the pituitary gland and the adrenal glands are crucial parts of the neuroendocrine system. This pathway is responsible for the regulation of stress reactions, energy storage and output, emotion and affect, sexuality, digestion and the immune system. MHC II major histocompatibility complex class II molecules are located on subclasses of antigen-presenting cells and display extracellular protein fragments to CD4 + helper T cells to determine the immune response. NF-κB nuclear factor κ light-chain enhancer of activated B cells is a transcription factor complex found in most animal cells that regulates cellular responses to infections and stress. Nup62 nucleoporin 62 is a complex of proteins that associates with the importin αβ complex of the nuclear pore to assist in the import of proteins with nuclear localization signals. PPIase activity peptidyl prolyl isomerase activity catalyzes cis – trans isomerization reactions of peptide bonds involving the amino acid proline. PPIase activity is required for the proper folding of several, but not all, proteins. Protein aggregation disorders agglomeration of proteins occurs in diseases such as Alzheimer's disease, bovine spongiform encephalopathy (mad cow disease) and Huntington's disease. Radicicol also known as monorden, radicicol is a macrolactone antibiotic that binds HSP90 and alters its function. It also inhibits tyrosine kinase and is anti-angiogenic. Reticulosyte lysate assembly system cell-free assembly system that contains all the eukaryotic cofactors necessary for steroid hormone receptor folding and allows for reconstitution of the receptors with chaperone complexes in vitro . Tau tau proteins are found primarily in neurons of the central nervous system and normally help in microtubule stabilization. Defective folding of tau and the resultant agglomeration are associated with neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. TPR domain the tetratricopeptide repeat is a structural motif used in protein–protein interactions. The TPR domains on FKBP51 and FKBP52 bind specifically to the extreme C terminus of HSP90. | ||
| 593 | |a The Border Biomedical Research Center and Department of Biological Sciences, University of Texas at El Paso, El Paso, TX 79968, United States | ||
| 593 | |a Departments of Molecular Medicine and Psychiatry, University of South Florida Alzheimer's Institute, Tampa, FL 33613, United States | ||
| 593 | |a Instituto de Biología y Medicina Experimental (IBYME), CONICET (1428ADN) Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales (C1428EGA) Universidad de Buenos Aires, Buenos Aires, Argentina | ||
| 593 | |a Max Planck Institute of Psychiatry, 80804 Munich, Germany | ||
| 690 | 1 | 0 | |a ANDROGEN RECEPTOR |
| 690 | 1 | 0 | |a ANTINEOPLASTIC AGENT |
| 690 | 1 | 0 | |a DOXORUBICIN |
| 690 | 1 | 0 | |a ESTROGEN RECEPTOR |
| 690 | 1 | 0 | |a IMMUNOGLOBULIN ENHANCER BINDING PROTEIN |
| 690 | 1 | 0 | |a MINERALOCORTICOID RECEPTOR |
| 690 | 1 | 0 | |a MULTIPROTEIN COMPLEX |
| 690 | 1 | 0 | |a PROGESTERONE RECEPTOR |
| 690 | 1 | 0 | |a PROTEIN FKBP51 |
| 690 | 1 | 0 | |a PROTEIN FKBP52 |
| 690 | 1 | 0 | |a PROTEIN KINASE B |
| 690 | 1 | 0 | |a RECEPTOR CHAPERONE COMPLEX |
| 690 | 1 | 0 | |a REGULATOR PROTEIN |
| 690 | 1 | 0 | |a STEROID HORMONE |
| 690 | 1 | 0 | |a STEROID RECEPTOR |
| 690 | 1 | 0 | |a TACROLIMUS |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ALZHEIMER DISEASE |
| 690 | 1 | 0 | |a ANXIETY DISORDER |
| 690 | 1 | 0 | |a BIPOLAR DISORDER |
| 690 | 1 | 0 | |a BREAST CARCINOGENESIS |
| 690 | 1 | 0 | |a BREAST TUMOR |
| 690 | 1 | 0 | |a CELL PROLIFERATION |
| 690 | 1 | 0 | |a CELLULAR DISTRIBUTION |
| 690 | 1 | 0 | |a COMPLEX FORMATION |
| 690 | 1 | 0 | |a DEPRESSION |
| 690 | 1 | 0 | |a DISEASE ASSOCIATION |
| 690 | 1 | 0 | |a DRUG TARGETING |
| 690 | 1 | 0 | |a GENITAL SYSTEM |
| 690 | 1 | 0 | |a HUMAN |
| 690 | 1 | 0 | |a IMMUNE SYSTEM |
| 690 | 1 | 0 | |a IMMUNOPATHOLOGY |
| 690 | 1 | 0 | |a MENTAL STRESS |
| 690 | 1 | 0 | |a METABOLIC DISORDER |
| 690 | 1 | 0 | |a MOLECULAR PATHOLOGY |
| 690 | 1 | 0 | |a NEUROPATHOLOGY |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PATHOPHYSIOLOGY |
| 690 | 1 | 0 | |a POSTTRAUMATIC STRESS DISORDER |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROSTATE CANCER |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a PROTEIN FOLDING |
| 690 | 1 | 0 | |a PROTEIN FUNCTION |
| 690 | 1 | 0 | |a PROTEIN LOCALIZATION |
| 690 | 1 | 0 | |a PROTEIN PROTEIN INTERACTION |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a REVIEW |
| 690 | 1 | 0 | |a SCHIZOPHRENIA |
| 690 | 1 | 0 | |a SIGNAL TRANSDUCTION |
| 690 | 1 | 0 | |a TAUOPATHY |
| 690 | 1 | 0 | |a ALZHEIMER DISEASE |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a HUMANS |
| 690 | 1 | 0 | |a MOLECULAR CHAPERONES |
| 690 | 1 | 0 | |a MOLECULAR TARGETED THERAPY |
| 690 | 1 | 0 | |a NEOPLASMS |
| 690 | 1 | 0 | |a PROTEIN TRANSPORT |
| 690 | 1 | 0 | |a RECEPTORS, STEROID |
| 690 | 1 | 0 | |a SIGNAL TRANSDUCTION |
| 690 | 1 | 0 | |a STRESS, PSYCHOLOGICAL |
| 690 | 1 | 0 | |a TACROLIMUS BINDING PROTEINS |
| 653 | 0 | 0 | |a fk 506 |
| 700 | 1 | |a Dickey, C.A. | |
| 700 | 1 | |a Galigniana, M.D. | |
| 700 | 1 | |a Rein, T. | |
| 700 | 1 | |a Cox, M.B. | |
| 773 | 0 | |d 2011 |g v. 22 |h pp. 481-490 |k n. 12 |p Trends Endocrinol. Metab. |x 10432760 |w (AR-BaUEN)CENRE-7077 |t Trends in Endocrinology and Metabolism | |
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| 856 | 4 | 0 | |u https://doi.org/10.1016/j.tem.2011.08.001 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_10432760_v22_n12_p481_Storer |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10432760_v22_n12_p481_Storer |y Registro en la Biblioteca Digital |
| 961 | |a paper_10432760_v22_n12_p481_Storer |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 999 | |c 71044 | ||