Physiological role for the cochaperone FKBP52 in androgen receptor signaling

Cheung-Flynn, Joyce; Prapapanich, Viravan; Cox, Marc B.; Riggs, Daniel L.; Suarez-Quian, Carlos; Smith, David F.

doi:10.1210/me.2005-0071

Cited by 215Heat shock proteins researchProstate Cancer Treatment and ResearchSperm and Testicular Function

Physiological role for the cochaperone FKBP52 in androgen receptor signaling

Open access

Cheung-Flynn, Joyce, Prapapanich, Viravan, Cox, Marc B., Riggs, Daniel L., Suarez-Quian, Carlos, Smith, David F.·2005·Molecular Endocrinology

DOI 10.1210/me.2005-0071

Open this paper in CoChat — free account Open PDF

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1210/me.2005-0071

Cites

44 of 44 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

FKBP52 functionally interacts with AR, GR and PR.
“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]
The ‘FKBP52 and AR Function’ section reports that FKBP52 enhances AR activity and notes a similar earlier observation with a GR reporter strain. Our copy does not establish a functional interaction with PR; a search for ‘progesterone receptor’ found it only in a reference title. The citation therefore supports AR and GR, but not the full three-receptor claim. (LLM, conf=0.88)
Experimental — accuracy not yet measured
FKBP52 knockout mice have developmental defects in reproductive tissues in males consistent with reduced AR signaling and failure of embryo implantation in females consistent with reduced PR signaling.
“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]
The “52KO Mice” section reports developmental abnormalities in male reproductive organs, and “How Is AR Function Altered by FKBP52?” links abnormal androgen-target tissue development to possible reduced AR responsiveness. The passages found in our copy do not report failed embryo implantation in females or link it to reduced PR signaling; searches for female implantation and progesterone-receptor terms did not find support for that part. (LLM, conf=0.88)
Experimental — accuracy not yet measured
The FKBP51 knockout mouse does not display overt defects in androgen signaling.
“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]
The “52KO Mice” section describes an FKBP52 knockout with reproductive defects, not an FKBP51 knockout. Searches for FKBP51, Fkbp5, and 51KO found no passage in our copy addressing whether FKBP51-knockout mice have overt defects in androgen signaling. (LLM, conf=0.76)
Experimental — accuracy not yet measured
FKBP51 is not required for AR function in development of the male mouse reproductive system.
“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]
The 52KO Mice and Discussion sections report that loss of FKBP52 impairs male reproductive development, but they do not establish whether FKBP51 is required for AR function. A search for FKBP51 found discussion of its expression alongside other chaperones, not a test of its requirement in male mice. (LLM, conf=0.73)
Experimental — accuracy not yet measured
FKBP52 is a positive regulator of GR, PR, and AR, but not ER or MR.
“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]

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.
“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]
Given the androgen, progesterone and glucocorticoid insensitivity phenotypes observed in fkbp52-deficient mice, FKBP52 is likely to have an important role and to serve as a therapeutic target in a variety of diseases dependent on these hormone signaling pathways.
“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]
Male mice with targeted ablation of FKBP52 are infertile due to hypospadias.
“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
FKBP52 is essential to AR activity in the prostate.
“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]
Only select AR-controlled tissues were affected in male FKBP52 KO animals, most notably the prostate gland.
“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]
FKBP52KO males show prostate dysgenesis and dramatically reduced AR activity at both endogenous and heterologous genes.
“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]
Loss of FKBP52 causes male infertility through a selective abrogation of AR activity while apparently leaving all other steroid receptor processes in the male unchanged.
“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]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
Mumberg, D., Müller, R., & Funk, M. (1995) · Gene · doi:10.1016/0378-1119(95)00037-7 · Cited by 1,972 · see citing works
Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery
Pratt, W. B., & Toft, D. O. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800201 · Cited by 1,478 · see citing works
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 1,436 · see citing works
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× · see citing works
“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.”
Method
FK506-binding Proteins 51 and 52 Differentially Regulate Dynein Interaction and Nuclear Translocation of the Glucocorticoid Receptor in Mammalian Cells
Wochnik, 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 · see citing works
International trends in rates of hypospadias and cryptorchidism.
Paulozzi, L. J. (1999) · Environmental Health Perspectives · doi:10.1289/ehp.99107297 · Cited by 469 · see citing works
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 · see citing works
Peptidylprolyl Cis / Trans Isomerases (Immunophilins): Biological Diversity - Targets - Functions
Galat, A. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033451862 · Cited by 360 · see citing works
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 · see citing works
Self-citation
Phenotypic Features, Androgen Receptor Binding, and Mutational Analysis in 278 Clinical Cases Reported as Androgen Insensitivity Syndrome1
Ahmed, 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 · see citing works
Dynamics of heat shock protein 90–progesterone receptor binding and the disactivation loop model for steroid receptor complexes
Smith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300 · see citing works
Structural Basis for Androgen Receptor Interdomain and Coactivator Interactions Suggests a Transition in Nuclear Receptor Activation Function Dominance
He, B., Gampe, R. T., Kole, A. J., Hnat, A. T., Stanley, T. B., An, G., Stewart, E. L., Kalman, R. I., Minges, J. T., & Wilson, E. M. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.036 · Cited by 291 · see citing works
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
Pratt, W. B., Galigniana, M. D., Harrell, J. M., & DeFranco, D. B. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.02.004 · Cited by 285 · see citing works
Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer
Langley, E., Zhou, Z.-X., & Wilson, E. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.50.29983 · Cited by 280 · see citing works
Androgen receptor distribution in rat testis: new implications for androgen regulation of spermatogenesis
Vornberger, W., Prins, G. S., Musto, N. A., & Suarez‐Quian, C. A. (1994) · Endocrinology · doi:10.1210/endo.134.5.8156934 · Cited by 268 · see citing works
Phenotypic Features, Androgen Receptor Binding, and Mutational Analysis in 278 Clinical Cases Reported as Androgen Insensitivity Syndrome
Ahmed, S. F. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.85.2.658 · Cited by 267 · see citing works
A 59-kilodalton protein associated with progestin, estrogen, androgen and glucocorticoid receptors
Tai, P. K. K., Maeda, Y., Nakao, K., Wakim, N. G., Duhring, J. L., & Faber, L. E. (1986) · Biochemistry · doi:10.1021/bi00366a043 · Cited by 257 · see citing works
Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes.
Peattie, D. A., Harding, M. W., Fleming, M. A., DeCenzo, M. T., Lippke, J. A., Livingston, D. J., & Benasutti, M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10974 · Cited by 251 · see citing works
Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity
Langley, E., Kemppainen, J. A., & Wilson, E. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.92 · Cited by 233 · see citing works
Hsp90 Regulates Androgen Receptor Hormone Binding Affinity in Vivo
Fang, Y., Fliss, A., Robins, D. M., & Caplan, A. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28697 · Cited by 227 · see citing works
Functional Interactions of the AF-2 Activation Domain Core Region of the Human Androgen Receptor with the Amino-Terminal Domain and with the Transcriptional Coactivator TIF2 (Transcriptional Intermediary Factor 2)
Berrevoets, C., Doesburg, P., Steketee, K., Trapman, J., & Brinkmann, A. O. (1998) · Molecular Endocrinology · doi:10.1210/mend.12.8.0153 · Cited by 212 · see citing works
Functional in Vivo Interaction between the Amino-Terminal, Transactivation Domain and the Ligand Binding Domain of the Androgen Receptor
Doesburg, P., Kuil, C. W., Berrevoets, C., Steketee, K., Faber, P. W., Mulder, E., Brinkmann, A. O., & Trapman, J. (1997) · Biochemistry · doi:10.1021/bi961775g · Cited by 209 · see citing works
Molecular Cloning of Human FKBP51 and Comparisons of Immunophilin Interactions with Hsp90 and Progesterone Receptor
Nair, S. C., Rimerman, R. A., Toran, E. J., Chen, S., Prapapanich, V., Butts, R. N., & Smith, D. F. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.2.594 · Cited by 194 · see citing works
Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex.
Scherrer, L. C., Dalman, F. C., Massa, E., Meshinchi, S., & Pratt, W. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45746-8 · Cited by 186 · see citing works
Functional analysis of the hsp90-associated human peptidyl prolyl Cis/Trans isomerases FKBP51, FKBP52 and cyp40 1 1Edited by R. Huber
Pirkl, F., & Buchner, J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4595 · Cited by 179 · see citing works
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
Freeman, B. C., Felts, S. J., Toft, D. O., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.14.4.422 · Cited by 168 · see citing works
Tetratricopeptide repeat cochaperones in steroid receptor complexes
Smith, D. F. (2004) · Cell stress & chaperones (Print) · doi:10.1379/csc-31.1 · Cited by 156 · see citing works
Cooperative Assembly of Androgen Receptor into a Nucleoprotein Complex That Regulates the Prostate-specific Antigen Enhancer
Huang, W., Shostak, Y., Tarr, P. T., Sawyers, C. L., & Carey, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25756 · Cited by 154 · see citing works
Reproductive toxicology: current and future directions11Abbreviations: FSH, follicle-stimulating hormone; LH, luteinizing hormone; PAH, polycyclic aromatic hydrocarbon; DBP, di-n-butyl phthalate; DEHP, di-(2-ethylhexyl)phthlate; MEHP, mono-2-(ethylhexyl)phthlate; DDT, dichlorodiphenyl-trichloroethane; p,p′-DDE, 1,1-dichloro-2,2-bis(p-chlorophenyl)ethylene; PCB, polychlorinated biphenyl; BPA, bisphenol A; and cAMP, cyclic AMP.
Hoyer, P. B. (2001) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00814-0 · Cited by 142 · see citing works
Immunophilin Chaperones in Steroid Receptor Signalling
Ratajczak, T., Ward, B. K., & Minchin, R. F. (2003) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026033451934 · Cited by 137 · see citing works
Unexpected Virilization in Male Mice Lacking Steroid 5 -Reductase Enzymes
Mahendroo, M., Cala, K. M., Hess, D. L., & Russell, D. W. (2001) · Endocrinology · doi:10.1210/endo.142.11.8510 · Cited by 133 · see citing works
p23, a simple protein with complex activities
Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116 · see citing works
FKBP52
Davies, T. H., & Sánchez, E. R. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.03.013 · Cited by 109 · see citing works
The role of 5α-reduction in steroid hormone physiology
Wilson, J. D. (2002) · Reproduction Fertility and Development · doi:10.1071/rd01074 · Cited by 104 · see citing works
Androgen receptor mutations and androgen insensitivity
McPhaul, M. J. (2002) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(02)00369-6 · Cited by 94 · see citing works
Overlapping Sites of Tetratricopeptide Repeat Protein Binding and Chaperone Activity in Heat Shock Protein 90
Ramsey, A. J., Russell, L. C., Whitt, S. R., & Chinkers, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001625200 · Cited by 79 · see citing works
The Biomarker and Endocrine Disruptors in Mammals
Choi, K., & Jeung, E. (2003) · Journal of Reproduction and Development · doi:10.1262/jrd.49.337 · Cited by 63 · see citing works
Partial androgen insensitivity with phenotypic variation caused by androgen receptor mutations that disrupt activation function 2 and the NH2- and carboxyl-terminal interaction
Quigley, C. A., Tan, J.-A., He, B., Zhou, Z.-X., Mébarki, F., Morel, Y., Forest, M. G., Chatelain, P., Ritzén, E. M., French, F. S., et al. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.08.007 · Cited by 57 · see citing works
The Heat Shock Protein 70 Cochaperone Hip Enhances Functional Maturation of Glucocorticoid Receptor
Nelson, G. M., Prapapanich, V., Carrigan, P. E., Roberts, P. J., Riggs, D. L., & Smith, D. F. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0054 · Cited by 57 · see citing works
Improved transduction of primary murine hepatocytes by recombinant adeno-associated virus 2 vectors in vivo
Zhong, L., Li, W., Yang, Z., Chen, L., Li, Y., Qing, K., Weigel-Kelley, K. A., Yöder, M. C., Shou, W., & Srivastava, A. (2004) · Gene Therapy · doi:10.1038/sj.gt.3302283 · Cited by 43 · see citing works
Molecular Defects of the Androgen Receptor
McPhaul, M. J. (2002) · Recent Progress in Hormone Research · doi:10.1210/rp.57.1.181 · Cited by 30 · see citing works
Dual roles of 90-kDa heat shock protein in the function of the mineralocorticoid receptor.
Nemoto, T., Ohara‐Nemoto, Y., Sato, N., & Ota, M. (1993) · PubMed · Cited by 28 · see citing works
Disorders of Androgen Biosynthesis
Miller, W. L. (2002) · Seminars in Reproductive Medicine · doi:10.1055/s-2002-35385 · Cited by 24 · see citing works
Specific cross-linking of the proline isomerase cyclophilin to a non-proline-containing peptide.
McNew, J. A., Sykes, K., & Goodman, J. M. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.2.223 · Cited by 17 · see citing works

Flagged first, then by citations

5 of the 49 references couldn’t be matched to a known paper.

Sorted by citations

Androgen Receptor (AR) Coregulators: A Diversity of Functions Converging on and Regulating the AR Transcriptional Complex
Heemers, H. V., & Tindall, D. J. (2007) · Endocrine Reviews · doi:10.1210/er.2007-0019 · Cited by 753 · see citing works
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 · see citing works
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 · see citing works
Hsp90: Structure and Function
Jackson, S. (2012) · Topics in current chemistry · doi:10.1007/128_2012_356 · Cited by 334 · see citing works
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 291 · see citing works
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 · see citing works
“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].”
Influential
Cooperative Interactions between Androgen Receptor (AR) and Heat-Shock Protein 27 Facilitate AR Transcriptional Activity
Zoubeidi, 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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citation
Molecular 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 · see citing works
Immunophilins: for the love of proteins
Barik, S. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6215-3 · Cited by 210 · see citing works
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 207 · see citing works
Chaperoning steroid hormone action
Picard, D. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.06.003 · Cited by 186 · see citing works
Minireview: The Intersection of Steroid Receptors with Molecular Chaperones: Observations and Questions
Smith, D. F., & Toft, D. O. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0089 · Cited by 173 · see citing works
Androgenetic Alopecia
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 · see citing works
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 · see citing works
The Molecular Chaperone Hsp90α Is Required for Meiotic Progression of Spermatocytes beyond Pachytene in the Mouse
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 · see citing works
Androgen resistance
Hughes, I. A., & Deeb, A. (2006) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2006.11.003 · Cited by 163 · see citing works
Modulation of Chaperone Function and Cochaperone Interaction by Novobiocin in the C-terminal Domain of Hsp90
Allan, R. K., Mok, D., Ward, B. K., & Ratajczak, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512406200 · Cited by 160 · see citing works
FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells
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 · see citing works
Essential role for co-chaperone Fkbp52 but not Fkbp51 in androgen receptor-mediated signaling and physiology
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 · see citing works
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 · see citing works
Noncatalytic Role of the FKBP52 Peptidyl-Prolyl Isomerase Domain in the Regulation of Steroid Hormone Signaling
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 · see citing works
Targeting the regulation of androgen receptor signaling by the heat shock protein 90 cochaperone FKBP52 in prostate cancer cells
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 · see citing works
FK506-Binding Proteins and Their Diverse Functions
Tong, M., & Jiang, Y. (2015) · Current Molecular Pharmacology · doi:10.2174/1874467208666150519113541 · Cited by 126 · see citing works
Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds
Dunyak, B. M., & Gestwicki, J. E. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00411 · Cited by 127 · see citing works
Modulation of glucocorticoid receptor nuclear translocation in neurons by immunophilins FKBP51 and FKBP52: Implications for major depressive disorder
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 · see citing works
Identification of candidate prostate cancer biomarkers in prostate needle biopsy specimens using proteomic analysis
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 · see citing works
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 · see citing works
FKBP52 deficiency–conferred uterine progesterone resistance is genetic background and pregnancy stage specific
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 · see citing works
FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform
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 · see citing works
“lished) and others (28) have found that AR hormone-”
BackgroundResult
CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70‐bound substrates
Stankiewicz, M., Nikolay, R., Rybin, V., & Mayer, M. P. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07737.x · Cited by 120 · see citing works
Receptor for activated C kinase 1 (RACK1) and Src regulate the tyrosine phosphorylation and function of the androgen receptor.
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 · see citing works
The 90-kDa Heat-shock Protein (Hsp90)-binding Immunophilin FKBP51 Is a Mitochondrial Protein That Translocates to the Nucleus to Protect Cells against Oxidative Stress
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 · see citing works
FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A
Periyasamy, S., Hinds, T., Shemshedini, L., Shou, W., & Sanchez, E. R. (2010) · Oncogene · doi:10.1038/onc.2009.458 · Cited by 108 · see citing works
“, 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.”
Background
Differential 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 106 · see citing works
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 · see citing works
Glucocorticoids, their uses, sexual dimorphisms, and diseases: new concepts, mechanisms, and discoveries
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 108 · see citing works
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 · see citing works
Molecular biology of androgen insensitivity
Jääskeläinen, J. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.08.006 · Cited by 98 · see citing works
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 · see citing works
Search for Potential Markers for Prostate Cancer Diagnosis, Prognosis and Treatment in Clinical Tissue Specimens Using Amine-Specific Isobaric Tagging (iTRAQ) with Two-Dimensional Liquid Chromatography and Tandem Mass Spectrometry
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 97 · see citing works
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 · see citing works
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 96 · see citing works
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 94 · see citing works
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 91 · see citing works
FKBP51 – a selective modulator of glucocorticoid and androgen sensitivity
Stechschulte, L. A., & Sanchez, E. R. (2011) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2011.04.012 · Cited by 92 · see citing works
Fluorescent Probes to Characterise FK506‐Binding Proteins
Kozany, C., März, A., Kress, C., & Hausch, F. (2009) · ChemBioChem · doi:10.1002/cbic.200800806 · Cited by 91 · see citing works
FKBP51 Null Mice Are Resistant to Diet-Induced Obesity and the PPARγ Agonist Rosiglitazone
Stechschulte, L. A., Qiu, B., Warrier, M., Hinds, T. D., Zhang, M., Gu, H., Xu, Y., Khuder, S. S., Russo, L., Najjar, S. M., et al. (2016) · Endocrinology · doi:10.1210/en.2015-1996 · Cited by 87 · see citing works
Unraveling the Dynamics of Estrogen and Progesterone Signaling in the Endometrium: An Overview
Silva, I. D. D., Wuidar, V., Zielonka, M., & Péqueux, C. (2024) · Cells · doi:10.3390/cells13151236 · Cited by 95 · see citing works
Control of Androgen Receptor Signaling in Prostate Cancer by the Cochaperone Small Glutamine–Rich Tetratricopeptide Repeat Containing Protein α
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 86 · see citing works
Subcellular Rearrangement of Hsp90-binding Immunophilins Accompanies Neuronal Differentiation and Neurite Outgrowth
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 · see citing works
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 · see citing works
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 · see citing works
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 78 · see citing works
The Immunophilin Ligands Cyclosporin A and FK506 Suppress Prostate Cancer Cell Growth by Androgen Receptor-Dependent and -Independent Mechanisms
Periyasamy, S., Warrier, M., Tillekeratne, M. P. M., Shou, W., & Sanchez, E. R. (2007) · Endocrinology · doi:10.1210/en.2007-0145 · Cited by 78 · see citing works
Regulation of the glucocorticoid response to stress‐related disorders by the Hsp90‐binding immunophilin FKBP51
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 75 · see citing works
FKBP4 connects mTORC2 and PI3K to activate the PDK1/Akt-dependent cell proliferation signaling in breast cancer
Mangé, A., Coyaud, É., Desmetz, C., Laurent, E., Béganton, B., Coopman, P., Raught, B., & Solassol, J. (2019) · Theranostics · doi:10.7150/thno.35561 · Cited by 66 · see citing works
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 73 · see citing works
Hsp90 Heterocomplexes Regulate Steroid Hormone Receptors: From Stress Response to Psychiatric Disease
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 73 · see citing works
Identification of Clinically Relevant Protein Targets in Prostate Cancer with 2D-DIGE Coupled Mass Spectrometry and Systems Biology Network Platform
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 · see citing works
Cotargeting Androgen Receptor and Clusterin Delays Castrate-Resistant Prostate Cancer Progression by Inhibiting Adaptive Stress Response and AR Stability
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 72 · see citing works
Modulating FKBP5/FKBP51 and autophagy lowers HTT (huntingtin) levels
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 72 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Deficiency of Immunophilin FKBP52 Promotes Endometriosis
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 · see citing works
FKBP4 is regulated by HOXA10 during decidualization and in endometriosis
Yang, H., Zhou, Y., Edelshain, B., Schatz, F., Lockwood, C. J., & Taylor, H. S. (2012) · Reproduction · doi:10.1530/rep-11-0438 · Cited by 63 · see citing works
Uterine FK506-binding protein 52 (FKBP52)–peroxiredoxin-6 (PRDX6) signaling protects pregnancy from overt oxidative stress
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 · see citing works
FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity
Cox, M. B., Riggs, D. L., Hessling, M., Schumacher, F., Buchner, J., & Smith, D. F. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0547 · Cited by 60 · see citing works
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90
Bracher, A., Kozany, C., Thost, A.-K., & Hausch, F. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911013862 · Cited by 62 · see citing works
Susceptibility to diet-induced hepatic steatosis and glucocorticoid resistance in FK506-binding protein 52-deficient mice
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 · see citing works
Dynamic mitochondrial-nuclear redistribution of the immunophilin FKBP51 is regulated by PKA signaling pathway to control gene expression in the process of adipocyte differentiation
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 · see citing works
Androgen Receptor Splice Variants are Resistant to Inhibitors of Hsp90 and FKBP52, which alter Androgen Receptor Activity and Expression
Shafi, A., Cox, M., & Weigel, N. (2013) · Steroids · doi:10.1016/j.steroids.2012.12.013 · Cited by 57 · see citing works
Progesterone receptor requires a co-chaperone for signalling in uterine biology and implantation
Tranguch, S. L., Smith, D. F., & Dey, S. K. (2006) · Reproductive BioMedicine Online · doi:10.1016/s1472-6483(10)60655-4 · Cited by 53 · see citing works
A heat shock protein 90 inhibitor that modulates the immunophilins and regulates hormone receptors without inducing the heat shock response
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 · see citing works
Identification of Differentially Expressed Proteins in Curcumin-Treated Prostate Cancer Cell Lines
Teiten, M.-H., Gaigneaux, A., Chateauvieux, S., Billing, A. M., Planchon, S., Fack, F., Renaut, J., Mack, F., Muller, C. P., Dicato, M. A., et al. (2012) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2011.0136 · Cited by 52 · see citing works
Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires
Pemberton, T. J. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-244 · Cited by 52 · see citing works
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 · see citing works
The Testes: Disorders of Sexual Differentiation and Puberty in the Male
Hughes, I. A. (2008) · Elsevier eBooks · doi:10.1016/b978-141604090-3.50021-1 · Cited by 50 · see citing works
Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions
Dean, M. E., & Johnson, J. L. (2020) · Cell Stress and Chaperones · doi:10.1007/s12192-020-01167-0 · Cited by 48 · see citing works
FKBP immunophilins and Alzheimer’s disease: A chaperoned affair
Cao, W., & Konsolaki, M. (2011) · Journal of Biosciences · doi:10.1007/s12038-011-9080-7 · Cited by 46 · see citing works
Crystal structures of the free and ligand-bound FK1–FK2 domain segment of FKBP52 reveal a flexible inter-domain hinge
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 · see citing works
Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities
Gurung, D., Danielson, J. A., Tasnim, A., Zhang, J.-T., Zou, Y., & Liu, J.-Y. (2023) · Biology · doi:10.3390/biology12071008 · Cited by 36 · see citing works
Identification of Male Gametogenesis Expressed Genes from the Scallop Nodipecten subnodosus by Suppressive Subtraction Hybridization and Pyrosequencing
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 · see citing works
Fkbp52 heterozygosity alters behavioral, endocrine and neurogenetic parameters under basal and chronic stress conditions in mice
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 · see citing works
Alterations in the steroid hormone receptor co-chaperone FKBPL are associated with male infertility: a case-control study
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 · see citing works
Promotion of Myoblast Differentiation by Fkbp5 via Cdk4 Isomerization
Ruiz-Estevez, M., Staats, J., Paatela, E., Munson, D., Katoku-Kikyo, N., Yuan, C., Asakura, Y., Hostager, R., Kobayashi, H., Asakura, A., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.006 · Cited by 39 · see citing works
“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).”
Background
Structure–Affinity Relationship Analysis of Selective FKBP51 Ligands
Feng, X., Sippel, C., Bracher, A., & Hausch, F. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00785 · Cited by 39 · see citing works
Testis Transcriptome Modulation in Klinefelter Patients with Hypospermatogenesis
D’Aurora, M., Ferlin, A., Garolla, A., Franchi, S., D’Onofrio, L., Trubiani, O., Palka, G., Foresta, C., Stuppia, L., & Gatta, V. (2017) · Scientific Reports · doi:10.1038/srep45729 · Cited by 40 · see citing works
Functional Drift of Sequence Attributes in the FK506-Binding Proteins (FKBPs)
Gałat, A. (2008) · Journal of Chemical Information and Modeling · doi:10.1021/ci700429n · Cited by 39 · see citing works
Targeted ablation reveals a novel role of FKBP52 in gene-specific regulation of glucocorticoid receptor transcriptional activity
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 · see citing works
Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins
Hildenbrand, Z. L., Molugu, S. K., Herrera, N., Ramirez, C., Xiao, C., & Bernal, R. A. (2011) · Oncotarget · doi:10.18632/oncotarget.225 · Cited by 38 · see citing works
FKBP51 and FKBP52 regulate androgen receptor dimerization and proliferation in prostate cancer cells
Maeda, K., Habara, M., Kawaguchi, M., Matsumoto, H., Hanaki, S., Masaki, T., Sato, Y., Matsuyama, H., Kunieda, K., Nakagawa, H., et al. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13030 · Cited by 32 · see citing works
Fkbp52 Regulates Androgen Receptor Transactivation Activity and Male Urethra Morphogenesis
Chen, H., Yong, W., Hinds, T. D., Yang, Z., Zhou, Y., Sánchez, E. R., & Shou, W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.156091 · Cited by 37 · see citing works
Caveolin-1 and Prostate Cancer Progression
Freeman, M. R., Yang, W., & Vizio, D. D. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-1222-9_7 · Cited by 37 · see citing works
The emerging role of FK506-binding proteins as cancer biomarkers: a focus on FKBPL
McKeen, H. D., Brennan, D. J., Hegarty, S. M., Lanigan, F. T., Jirström, K., Byrne, C., Yakkundi, A., McCarthy, H. O., Gallagher, W. M., & Robson, T. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390663 · Cited by 36 · see citing works

0888-8809/05/$15.00/0 Molecular Endocrinology 19(6):1654–1666 Printed in U.S.A. Copyright © 2005 by The Endocrine Society doi: 10.1210/me.2005-0071 Physiological Role for the Cochaperone FKBP52 in Androgen Receptor Signaling
Cheung-flynn, J., Prapapanich, V., Cox, M. B., Riggs, D. L., Suarez-quian, C., & Smith, D. F. (2005)
Self-citation
Essential role for co-chaperone Fkbp52 but not Fkbp51 in androgen receptor-mediated signaling and physiology
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 · see citing works
Essential Role for Co-chaperone Fkbp52 but Not Fkbp51 in
(2014)
RESEARCH ARTICLE The FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling
Samaniego, C., Suh, J. H., Chattopadhyay, A., Olivares, K., Guy, N. C., Sivils, J. C., Dey, P., Yumoto, F., Fletterick, R. J., Ström, A., et al. (2016)
A Genomic Approach To Assessing The FKBP52-Regulated Androgen Receptor Cistrome And Transcriptome
Ortiz, N. R. (2021) · scholarworks - UTEP (The University of Texas at El Paso)

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.
ORCID: Cox, Marc B.
Riggs, Daniel L.
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
DOI: 10.1210/me.2005-0071
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
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › 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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Physiological role for the cochaperone FKBP52 in androgen receptor signaling

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks