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Physiological Role for the Cochaperone FKBP52 in Androgen Receptor Signaling
Open accessAbstract
Molecular chaperones mediate multiple aspects of steroid receptor function, but the physiological importance of most receptor-associated cochaperones has not been determined. To help fill this gap, we targeted for disruption the mouse gene for the 52-kDa FK506 binding protein, FKBP52, a 90-kDa heat shock protein (Hsp90)-binding immunophilin found in steroid receptor complexes. A mouse line lacking FKBP52 (52KO) was generated and characterized. Male 52KO mice have several defects in reproductive tissues consistent with androgen insensitivity; among these defects are ambiguous external genitalia and dysgenic prostate. FKBP52 and androgen receptor (AR) are coexpressed in prostate epithelial cells of wild-type mice. However, FKBP52 and AR are similarly coexpressed in testis even though testis morphology and spermatogenesis in 52KO males are usually normal. Molecular studies confirm that FKBP52 is a component of AR complexes, and cellular studies in yeast and human cell models demonstrate that FKBP52 can enhance AR-mediated transactivation. AR enhancement requires FKBP52 peptidylprolyl isomerase activity as well as Hsp90-binding ability, and enhancement probably relates to an affect of FKBP52 on AR-folding pathways. In the presence of FKBP52, but not other cochaperones, the function of a minimally active AR point mutant can be dramatically restored. We conclude that FKBP52 is an AR folding factor that has critically important physiological roles in some male reproductive tissues.
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In the citing paper
“While FKBP52 is known to functionally interact with AR, GR and PR [6–8], β-catenin only interacts strongly with AR, but not GR and PR [20].”
From The FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling (2015) · cites this paper as [6]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“FKBP52 knockout mice have developmental defects in reproductive tissues (in males) consistent with reduced ARsignaling and a failure of embryo implantation (in females) consistent with reduced PR signaling (4, 37).”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [4]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Because the FKBP51 knockout mouse does not display overt defects in androgen signaling (4, 37), the contribution of FKBP51 to AR function has been unclear.”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [4]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“This is despite the fact that FKBP51 is not required for AR function in the development of the male mouse reproductive system, which instead relies on the closely related cochaperone FKBP52 (4, 37).”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [4]
Experimental — accuracy not yet measuredIn the citing paper
“FKBP52 is a positive regulator of glucocorticoid receptor (GR) [5], progesterone receptor (PR) [6], and androgen receptor (AR) [7], but not estrogen receptor (ER) or mineralocorticoid receptor (MR) [5].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [7]
In the citing paper
“Male 52KO mice display phenotypes consistent with partial androgen insensitivity including dysgenic prostate and seminal vesicles, ambiguous external genitalia including hypospadias, and retention of nipples into adulthood [7, 32].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [7]
In the citing paper
“Given the androgen, progesterone and glucocorticoid insensitivity phenotypes observed in the fkbp52-deficient mice [6, 7, 32, 35, 51], FKBP52 is likely to have an important role and to serve as a therapeutic target in a variety of diseases that are dependent on these hormone signaling pathways.”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [7]
In the citing paper
“Our laboratory (Yong et al., 2007) and others (Cheung-Flynn et al., 2005) have shown that male mice with targeted ablation of FKBP52 are infertile due to a developmental defect of the penis termed hypospadias – a condition prevalent in newborn boys and thought to arise from androgen insensitivity (Batch et al., 1992; Nakao et al., 1992).”
From FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A (2010) · cites this paper as Cheung-Flynn et al., 2005
In the citing paper
“suggesting that FKBP52 is an essential immunophilin controlling AR activity in these tissues.”
From The Immunophilin Ligands Cyclosporin A and FK506 Suppress Prostate Cancer Cell Growth by Androgen Receptor-Dependent and -Independent Mechanisms (2007) · cites this paper as [12]
In the citing paper
“Moreover, only select ARcontrolled tissues were affected in male FKBP52 KO animals, most notably the prostate gland.”
From The Immunophilin Ligands Cyclosporin A and FK506 Suppress Prostate Cancer Cell Growth by Androgen Receptor-Dependent and -Independent Mechanisms (2007) · cites this paper as [12]
In the citing paper
“Interestingly, FKBP52KO males also showed prostate dysgenesis, as well as dramatically reduced AR activity at both endogenous and heterologous genes (12,39).”
From The Immunophilin Ligands Cyclosporin A and FK506 Suppress Prostate Cancer Cell Growth by Androgen Receptor-Dependent and -Independent Mechanisms (2007) · cites this paper as [12]
In the citing paper
“In this case, loss of FKBP52 caused male infertility through a selective abrogation of AR activity, while apparently leaving all other steroid receptor processes in the male unchanged.”
From The Immunophilin Ligands Cyclosporin A and FK506 Suppress Prostate Cancer Cell Growth by Androgen Receptor-Dependent and -Independent Mechanisms (2007) · cites this paper as [12]
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Citations
Cites
Mumberg, D., Müller, R., & Funk, M. (1995) · Gene · doi:10.1016/0378-1119(95)00037-7 · Cited by 1,972
Pratt, W. B., & Toft, D. O. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800201 · Cited by 1,497
Androgen Receptor Defects: Historical, Clinical, and Molecular Perspectives*
Quigley, C. A., Bellis, A. D., Marschke, K. B., Awady, M. K. E., Wilson, E. M., & French, F. S. (1995) · Endocrine Reviews · doi:10.1210/edrv-16-3-271 · Cited by 1,459
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · cited 1×
“First, an established yeast model for steroid receptor function (19, 20) was employed to take advantage of the fact that Saccharomyces cerevisiae lacks an endogenous gene for the TPR-containing FKBP family members.”
MethodWochnik, G. M., Rüegg, J., Abel, G. A., Schmidt, U., Holsboer, F., & Rein, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m407498200 · Cited by 638
International trends in rates of hypospadias and cryptorchidism.
Paulozzi, L. J. (1999) · Environmental Health Perspectives · doi:10.1289/ehp.99107297 · Cited by 469
A New First Step in Activation of Steroid Receptors
Davies, T. H., Ning, Y.-M., & Sánchez, E. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100531200 · Cited by 427
Peptidylprolyl Cis / Trans Isomerases (Immunophilins): Biological Diversity - Targets - Functions
Galat, A. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033451862 · Cited by 360
The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
Riggs, D. L., Roberts, P. J., Chirillo, S. C., Cheung‐Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Picard, D., & Smith, D. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg108 · Cited by 353 · cited 8×
“Furthermore, a double point mutation (52-FD67DV) in the PPIase active site (20) also blocks potentiation, suggesting that the PPIase domain is required for enhancing AR function.”
BackgroundMethodResultInfluentialSelf-citationAhmed, S. F., Cheng, A. W.-F., Dovey, L., Hawkins, J. R., Martin, H., Rowland, J., Shimura, N., Tait, A. D., & Hughes, I. A. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.85.2.6337 · Cited by 315
Research works printed but not linked: 2
- Alberti, 2003, BAG-1—a nucleotide exchange factor of Hsc70 with multiple cellular functions., Cell Stress Chaperones, 8, 225, 10.1379/1466-1268(2003)008<0225:BNEFOH>2.0.CO;2 · DOI
- McDonough, 2003, CHIP: a link between the chaperone and proteasome systems., Cell Stress Chaperones, 8, 303, 10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2 · DOI
Cited by
Sorted by citations
Heemers, H. V., & Tindall, D. J. (2007) · Endocrine Reviews · doi:10.1210/er.2007-0019 · Cited by 753
The Aryl Hydrocarbon Receptor Complex and the Control of Gene Expression
Beischlag, T. V., Morales, J. L., Hollingshead, B. D., & Perdew, G. H. (2008) · Critical Reviews™ in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v18.i3.20 · Cited by 727
The glucocorticoid responses are shaped by molecular chaperones
Grad, I., & Picard, D. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.018 · Cited by 423
Jackson, S. (2012) · Topics in current chemistry · doi:10.1007/128_2012_356 · Cited by 347
Aetiology of hypospadias: a systematic review of genes and environment
van der Zanden, L. F. M., van Rooij, I. A. L. M., Feitz, W., Franke, B., Knoers, N. V. A. M., & Roeleveld, N. (2012) · Human Reproduction Update · doi:10.1093/humupd/dms002 · Cited by 298
FKBP51 and FKBP52 in signaling and disease
Storer, C. L., Dickey, C. A., Galigniana, M. D., Rein, T., & Cox, M. B. (2011) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.08.001 · Cited by 266
“The prostate dysgenesis observed in 52KO mice established FKBP52 as a critically important regulator of prostate development [7], and enhanced FKBP52 levels have been observed in prostate needle biopsies from human patients [52].”
InfluentialZoubeidi, A., Zardan, A., Beraldi, E., Fazli, L., Sowery, R. D., Rennie, P. S., Nelson, C. C., & Gleave, M. E. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2057 · Cited by 256
Versatile TPR domains accommodate different modes of target protein recognition and function
Allan, R. K., & Ratajczak, T. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0248-0 · Cited by 245
Selective inhibitors of the FK506-binding protein 51 by induced fit
Gaali, S., Kirschner, A., Cuboni, S., Hartmann, J., Kozany, C., Balsevich, G., Namendorf, C., Fernandez-Vizarra, P., Sippel, C., Zannas, A. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1699 · Cited by 245
The Genetic and Environmental Factors Underlying Hypospadias
Bouty, A., Ayers, K. L., Pask, A. J., Héloury, Y., & Sinclair, A. H. (2015) · Sexual Development · doi:10.1159/000441988 · Cited by 245
Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation
Tranguch, S., Cheung-Flynn, J., Daikoku, T., Prapapanich, V., Cox, M. B., Xie, H., Wang, H., Das, S. K., Smith, D. F., & Dey, S. K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505775102 · Cited by 232
Self-citationMolecular chaperones, essential partners of steroid hormone receptors for activity and mobility
Echeverría, P. C., & Picard, D. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.11.012 · Cited by 225
Immunophilins: for the love of proteins
Barik, S. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6215-3 · Cited by 218
46,XY disorders of sex development (DSD)
Mendonca, B. B., Domenice, S., Arnhold, I. J. P., & Costa, E. M. F. (2008) · Clinical Endocrinology · doi:10.1111/j.1365-2265.2008.03392.x · Cited by 209
Chaperoning steroid hormone action
Picard, D. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.06.003 · Cited by 190
Smith, D. F., & Toft, D. O. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0089 · Cited by 173
Otberg, N., Finner, A. M., & Shapiro, J. (2007) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2007.03.004 · Cited by 175
FKBP Ligands—Where We Are and Where to Go?
Kolos, J. M., Voll, A. M., Bauder, M., & Hausch, F. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01425 · Cited by 158
Grad, I., Cederroth, C. R., Walicki, J., Grey, C., Barluenga, S., Winssinger, N., de Massy, B., Nef, S., & Picard, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015770 · Cited by 171
Hughes, I. A., & Deeb, A. (2006) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2006.11.003 · Cited by 163
Allan, R. K., Mok, D., Ward, B. K., & Ratajczak, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512406200 · Cited by 160
Ni, L., Yang, C.-S., Gioeli, D., Frierson, H., Toft, D. O., & Paschal, B. M. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01891-08 · Cited by 155
Yong, W., Yang, Z., Periyasamy, S., Chen, H., Yucel, S., Li, W., Lin, L. Y., Wolf, I. M., Cohn, M. J., Baskin, L. S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609360200 · Cited by 156
Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle
Li, J., Richter, K., & Buchner, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1965 · Cited by 155
Riggs, D. L., Cox, M. B., Tardif, H. L., Hessling, M., Buchner, J., & Smith, D. F. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00985-07 · Cited by 150
De Leon, J. T., Iwai, A., Feau, C., Garcia, Y., Balsiger, H. A., Storer, C. L., Suro, R. M., Garza, K. M., Lee, S., Sang Kim, Y., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105160108 · Cited by 132
FK506-Binding Proteins and Their Diverse Functions
Tong, M., & Jiang, Y. (2015) · Current Molecular Pharmacology · doi:10.2174/1874467208666150519113541 · Cited by 135
Dunyak, B. M., & Gestwicki, J. E. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00411 · Cited by 127
Tatro, E. T., Everall, I. P., Kaul, M., & Achim, C. L. (2009) · Brain Research · doi:10.1016/j.brainres.2009.06.036 · Cited by 125
Lin, J., Xu, J., Tian, H., Gao, X., Chen, Q., Gu, Q., Xu, G., Song, J., & Zhao, F. (2007) · International Journal of Cancer · doi:10.1002/ijc.23016 · Cited by 125
Androgens and mammalian male reproductive tract development
Murashima, A., Kishigami, S., Thomson, A. A., & Yamada, G. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.020 · Cited by 121
Tranguch, S., Wang, H., Daikoku, T., Xie, H., Smith, D. F., & Dey, S. K. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31622 · Cited by 121
Yang, Z., Wolf, I. M., Chen, H., Periyasamy, S., Chen, Z., Yong, W., Shi, S., Zhao, W., Xu, J., Srivastava, A., et al. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0024 · Cited by 119
“lished) and others (28) have found that AR hormone-”
BackgroundResultStankiewicz, M., Nikolay, R., Rybin, V., & Mayer, M. P. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07737.x · Cited by 120
Kraus, S., Gioeli, D., Vomastek, T., Gordon, V., & Weber, M. J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0596 · Cited by 118
Gallo, L. I., Lagadari, M., Piwien‐Pilipuk, G., & Galigniana, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.256610 · Cited by 110
Periyasamy, S., Hinds, T., Shemshedini, L., Shou, W., & Sanchez, E. R. (2010) · Oncogene · doi:10.1038/onc.2009.458 · Cited by 108
“, 2007) and in others (Cheung-Flynn et al., 2005) have shown that male mice with targeted ablation of FKBP52 are infertile because of a developmental defect of the penis termed hypospadias—a condition prevalent in newborn boys and thought to arise from androgen insensitivity (Batch et al.”
BackgroundDifferential Impact of Tetratricopeptide Repeat Proteins on the Steroid Hormone Receptors
Schülke, J.-P., Wochnik, G. M., Lang‐Rollin, I., Gassen, N. C., Knapp, R., Berning, B., Yassouridis, A., & Rein, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011717 · Cited by 109
Multidomain Peptidyl Prolyl cis/trans Isomerases
Schiene‐Fischer, C. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.11.012 · Cited by 103
Martinez, G. J., Appleton, M., Kipp, Z. A., Loria, A. S., Min, B., & Hinds, T. D. (2023) · Physiological Reviews · doi:10.1152/physrev.00021.2023 · Cited by 115
Protein Kinase CK2 in Health and Disease: CK2: The kinase controlling the Hsp90 chaperone machinery
Miyata, Y. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-9152-0 · Cited by 98
Molecular biology of androgen insensitivity
Jääskeläinen, J. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.08.006 · Cited by 101
Progesterone receptor signaling in the initiation of pregnancy and preservation of a healthy uterus
Wetendorf, M., & DeMayo, F. J. (2014) · The International Journal of Developmental Biology · doi:10.1387/ijdb.140069mw · Cited by 101
Garbis, S. D., Tyritzis, S. Ι., Roumeliotis, T. I., Zerefos, P. G., Γιαννοπούλου, Ε., Vlahou, A., Κοσσίδα, Σ., Diaz, J. I., Vourekas, S., Tamvakopoulos, C., et al. (2008) · Journal of Proteome Research · doi:10.1021/pr800060r · Cited by 96
NF-κB Transcriptional Activity Is Modulated by FK506-binding Proteins FKBP51 and FKBP52
Erlejman, A. G., Leo, S. A. D., Mazaira, G. I., Molinari, A. M., Camisay, M. F., Fontana, V. A., Cox, M. B., Piwien‐Pilipuk, G., & Galigniana, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.582882 · Cited by 98
Chaperoning steroidal physiology: Lessons from mouse genetic models of Hsp90 and its cochaperones
Sánchez, E. R. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.006 · Cited by 98
Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52
Zgajnar, N. R., Leo, S. A. D., Lotufo, C. M., Erlejman, A. G., Piwien‐Pilipuk, G., & Galigniana, M. D. (2019) · Biomolecules · doi:10.3390/biom9020052 · Cited by 95
The Hsp90 Cochaperone p23 Is Essential for Perinatal Survival
Grad, I., McKee, T., Ludwig, S. M., Hoyle, G. W., Ruíz, P., Wurst, W., Floß, T., Miller, C. A., & Picard, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00734-06 · Cited by 93
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Stechschulte, L. A., & Sanchez, E. R. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.04.012 · Cited by 92
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Kozany, C., März, A., Kress, C., & Hausch, F. (2009) · ChemBioChem · doi:10.1002/cbic.200800806 · Cited by 91
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Buchanan, G., Ricciardelli, C., Harris, J. M., Prescott, J., Yu, Z. C.-L., Li, J., Butler, L. M., Marshall, V. R., Scher, H. I., Gerald, W. L., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1646 · Cited by 87
Quintá, H., Maschi, D., Gomez-Sanchez, C., Piwien-Pilipuk, G., & Galigniana, M. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06970.x · Cited by 86
The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation
Chambraud, B., Belabes, H., Fontaine‐Lenoir, V., Fellous, A., & Baulieu, E. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-7667com · Cited by 85
Regulation of steroid hormone receptor function by the 52-kDa FK506-binding protein (FKBP52)
Sivils, J. C., Storer, C. L., Galigniana, M. D., & Cox, M. B. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.03.010 · Cited by 81
Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies
Shelton, L. B., Koren, J., & Blair, L. J. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00724 · Cited by 80
Periyasamy, S., Warrier, M., Tillekeratne, M. P. M., Shou, W., & Sanchez, E. R. (2007) · Endocrinology · doi:10.1210/en.2007-0145 · Cited by 78
Galigniana, N. M., Ballmer, L. T., Toneatto, J., Erlejman, A. G., Lagadari, M., & Galigniana, M. D. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07775.x · Cited by 76
Mangé, A., Coyaud, É., Desmetz, C., Laurent, E. M. N., Béganton, B., Coopman, P. J., Raught, B., & Solassol, J. (2019) · Theranostics · doi:10.7150/thno.35561 · Cited by 77
Diverse structures, functions and uses of FK506 binding proteins
Bonner, J. M., & Boulianne, G. L. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.06.013 · Cited by 78
Baker, J. D., McMillan, I. O., Ospina, S. R., Gulick, D., & Blair, L. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010079 · Cited by 74
Ummanni, R., Mundt, F., Pospisil, H., Venz, S., Scharf, C., Barett, C., Fälth, M., Köllermann, J. W., Walther, R., Schlomm, T., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016833 · Cited by 74
Matsumoto, H., Yamamoto, Y., Shiota, M., Kuruma, H., Beraldi, E., Matsuyama, H., Zoubeidi, A., & Gleave, M. E. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0359 · Cited by 73
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Bailus, B. J., Scheeler, S. M., Simons, J., Sanchez, M. A., Tshilenge, K., Creus‐Muncunill, J., Naphade, S. B., Lopez‐Ramirez, A., Zhang, N., Madushani, K. L., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1904489 · Cited by 75
The role of sonic hedgehog-Gli2 pathway in the masculinization of external genitalia.
Miyagawa, S., Matsumaru, D., Murashima, A., Omori, A., Satoh, Y., Haraguchi, R., Motoyama, J., Iguchi, T., Nakagata, N., Hui, C.-C., et al. (2011) · Endocrinology · doi:10.1210/en.2011-0263 · Cited by 78
Pharmacologic Unmasking of Epigenetically Silenced Genes in Breast Cancer
Ostrow, K. L., Park, H. L., Hoque, M. O., Kim, M. S., Liu, J.-W., Argani, P., Westra, W. H., Criekinge, W. V., & Sidransky, D. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1304 · Cited by 71
Mini-review: Foldosome regulation of androgen receptor action in prostate cancer
Cano, L. Q., Lavery, D. N., & Bevan, C. L. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.01.023 · Cited by 70
FKBP family proteins as promising new biomarkers for cancer
Solassol, J., Mangé, A., & Maudelondé, T. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.03.012 · Cited by 67
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Hirota, Y., Tranguch, S., Daikoku, T., Hasegawa, A., Osuga, Y., Taketani, Y., & Dey, S. K. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.080527 · Cited by 67
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Hirota, Y., Acar, N., Tranguch, S., Burnum, K. E., Xie, H., Kodama, A., Osuga, Y., Ustunel, I., Friedman, D. B., Caprioli, R. M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009324107 · Cited by 62
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Warrier, M., Hinds, T. D., Ledford, K. J., Cash, H. A., Patel, P. R., Bowman, T. A., Stechschulte, L. A., Yong, W., Shou, W., Najjar, S. M., et al. (2010) · Endocrinology · doi:10.1210/en.2009-1158 · Cited by 57
Toneatto, J., Guber, S., Charó, N. L., Susperreguy, S., Schwartz, J., Galigniana, M. D., & Piwien‐Pilipuk, G. (2013) · Journal of Cell Science · doi:10.1242/jcs.125799 · Cited by 55
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McConnell, J. R., Alexander, L. A., & McAlpine, S. R. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.11.059 · Cited by 52
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Pemberton, T. J. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-244 · Cited by 52
46,XY Disorders of Sexual Development
Domenice, S., Arnhold, I. J. P., Costa, E. M. F., & Mendonca, B. B. (2013) · Europe PMC (PubMed Central) · Cited by 52
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Hughes, I. A. (2008) · Elsevier eBooks · doi:10.1016/b978-141604090-3.50021-1 · Cited by 50
Dean, M. E., & Johnson, J. L. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01167-0 · Cited by 48
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Bracher, A., Kozany, C., Hähle, A., Wild, P., Zacharias, M., & Hausch, F. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.07.041 · Cited by 45
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Llera‐Herrera, R., Garcı́a-Gasca, A., Abreu‐Goodger, C., Huvet, A., & Ibarra, A. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073176 · Cited by 43
Hartmann, J., Wagner, K. V., Dedic, N., Marinescu, D., Scharf, S. H., Wang, X., Deussing, J. M., Hausch, F., Rein, T., Schmidt, U., et al. (2012) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2012.04.017 · Cited by 42
Sunnotel, O., Hiripi, L., Lagan, K., McDaid, J. R., Leon, J. T. D., Miyagawa, Y., Crowe, H., Kaluskar, S., Ward, M. S., Scullion, C. A., et al. (2010) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-8-22 · Cited by 43
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“Fkbp4−/− male mice are also sterile with multiple defects in reproductive tissues, such as ambiguous external genitalia and prostate dysgenesis, due to disrupted androgen receptor signaling (Cheung-Flynn et al., 2005).”
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Wolf, I. M., Periyasamy, S., Hinds, T., Yong, W., Shou, W., & Sanchez, E. R. (2009) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.11.006 · Cited by 38
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Metadata
- Authors
- Cheung-Flynn, J., Prapapanich, V., Cox, M. B., Riggs, D. L., Suarez-Quian, C., & Smith, D. F.
- Affiliations
- Department of Biochemistry and Molecular Biology (J.C.-F., V.P., M.B.C., D.L.R., D.F.S.), Mayo Clinic College of Medicine, Scottsdale, Arizona 85259
- Mayo Clinic (US)
- Department of Cell Biology (C.S.-Q.), Georgetown University Medical Center, Washington, D.C. 20057
- Corresponding author
- Smith, David F.
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2005-06-01
- Volume
- 19
- Issue
- 6
- Pages
- 1654-1666
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- OpenAlex
- W2109243666
- Cited by
- 212
- References
- 49
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3 · 2023: 8 · 2022: 6 · 2021: 6 · 2020: 5 · 2019: 7 · 2018: 5 · 2017: 8 · 2016: 10 · 2015: 9 · 2014: 13 · 2013: 15 · 2012: 20
- FWCI
- 6.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Nebraska Medical Center
- Mayo Foundation for Medical Education and Research
- National Institutes of Health
- U.S. Public Health Service (R01-48218)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Prostate Cancer Treatment and Research
- Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
- Keywords
- FKBP52, androgen receptor, co-chaperones, immunophilins, peptidylprolyl isomerase, steroid receptor signaling, androgen insensitivity syndrome, ambiguous genitalia, receptor folding, transcriptional activation
- MeSH terms
- Animals, Dose-Response Relationship, Drug, Genetic Vectors, Genotype, Humans, Immunohistochemistry, Male, Models, Genetic, Models, Molecular, Plasmids, Proline, Prostate, Protein Binding, Protein Conformation, Receptors, Androgen, Testis, Tissue Distribution, Blotting, Western, Signal Transduction, Transcriptional Activation, Gene Deletion, Point Mutation, Protein Structure, Tertiary, Protein Folding, Mice, Knockout, Molecular Chaperones, HSP90 Heat-Shock Proteins, Tacrolimus Binding Proteins, Mice
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