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The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
Open accessAbstract
Hsp90 is required for the normal activity of steroid receptors, and in steroid receptor complexes it is typically bound to one of the immunophilin-related co-chaperones: the peptidylprolyl isomerases FKBP51, FKBP52 or CyP40, or the protein phosphatase PP5. The physiological roles of the immunophilins in regulating steroid receptor function have not been well defined, and so we examined in vivo the influences of immunophilins on hormone-dependent gene activation in the Saccharomyces cerevisiae model for glucocorticoid receptor (GR) function. FKBP52 selectively potentiates hormone-dependent reporter gene activation by as much as 20-fold at limiting hormone concentrations, and this potentiation is readily blocked by co-expression of the closely related FKBP51. The mechanism for potentiation is an increase in GR hormone-binding affinity that requires both the Hsp90-binding ability and the prolyl isomerase activity of FKBP52.
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“Previous studies in yeast demonstrated that FKBP52 binding to Hsp90 is required for regulation of AR activity [7].”
From The FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling (2015) · cites this paper as [7]
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“In contrast, FKBP52 enhances GR, PR, and AR responsiveness to cognate hormone (28).”
From FKBP51 Promotes Assembly of the Hsp90 Chaperone Complex and Regulates Androgen Receptor Signaling in Prostate Cancer Cells (2010) · cites this paper as [28]
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“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 [7]
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In the citing paper
“FKBP51 inhibits GR ligand binding, nuclear translocation and transcriptional activity, while FKBP52 potentiates each of these fundamental GR activities22–32.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [23]
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In the citing paper
“unlike FKBP52, FKBP51 does not enhance GR ligand binding in vitro, consistent with in vivo studies23,27,29.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [23]
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“Thus, the relative concentrations of FKBP51 and FKBP52 in the cell dictate the level of GR activity in vivo23,28,55.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [23]
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“The co-expression of FKBP52 (K354A), which completely lacks Hsp90 binding [7], with β-catenin (S33A) also resulted in the synergistic up-regulation of AR-mediated luciferase reporter expression comparable to that observed with wild type FKBP52 both in the presence and absence of hormone (Fig 5B).”
From The FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling (2015) · cites this paper as [7]
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“However, FKBP51 does not potentiate GR ligand binding in any of these conditions, unlike FKBP52, recapitulating in vivo findings23,29.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [23]
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“strongly suggesting FKBP52 potentiates the GR ligand binding affinity beyond the minimal chaperone mixture, consistent with reports in vivo23.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [23]
In 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 [5]
In the citing paper
“The fact that FKBP52 regulation has been localized to the receptor ligand binding domain (LBD) [5, 15] suggests that the FK1 interaction partner is the receptor LBD.”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [5]
In the citing paper
“The FK1 domain facilitates binding to the immunosuppressive drug FK506, confers PPIase activity [3], and is the primary regulatory domain for SHRs [5].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [5]
In the citing paper
“The FKBPs compete for binding to the SHR complex and, as a result, overexpression of FKBP51 decreases receptor regulation by FKBP52 [5]”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [5]
In the citing paper
“The FK1 domain is deemed critical for receptor potentiation by FKBP52 [5], but its enzymatic activity is not required for this potentiation. Domain integrity in and around the PPIase pocket is essential [9].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [5]
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Citations
Cites
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Cited by
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Items 201–300 of 358
Imai, A., Sahara, H., Tamura, Y., Jimbow, K., Saito, T., Ezoe, K., Yotsuyanagi, T., & Sato, N. (2007) · European Journal of Immunology · doi:10.1002/eji.200636392 · Cited by 25
Tetratricopeptide Repeat Domain 9A Negatively Regulates Estrogen Receptor Alpha Activity
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“Although TTC9A does not bind to ERα or its chaperone protein Hsp90 directly, TTC9A strongly interacts with FKBP38 and FKBP51, both of which interact with ERα and Hsp90 and modulate ERα activity.”
BackgroundInfluentialAgam, G., Atawna, B., Damri, O., & Azab, A. N. (2024) · Cells · doi:10.3390/cells13100801 · Cited by 25
“In most studies, FKBP51 is observed as a negative regulator of steroid hormone receptor activity, while FKBP52 positively regulates the activity of most of the steroid hormone receptors, except for estrogen receptor/mineralocorticoid receptor activity [14–17].”
BackgroundWheat Bax Inhibitor-1 interacts with TaFKBP62 and mediates response to heat stress
Lu, P.-P., Zheng, W., Wang, C.-T., Shi, W., Fu, J., Chen, M., Chen, J., Zhou, Y., Xi, Y., & Xu, Z. (2018) · BMC Plant Biology · doi:10.1186/s12870-018-1485-0 · Cited by 23
Regulation of FKBP51 and FKBP52 functions by post-translational modifications
Daneri-Becerra, C., Zgajnar, N. R., Lotufo, C. M., Ramos-Hryb, A. B., Piwien‐Pilipuk, G., & Galigniana, M. D. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190334 · Cited by 23
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“Nevertheless, the limitations of the low sensitivity of the yeast receptor assays have been addressed by introducing the co-chaperones FKBP52 and HIP, resulting in enhanced GR reporter gene activation (Nelson et al. 2004; Riggs et al. 2003).”
BackgroundBaischew, A., Engel, S., Taubert, M. C., Geiger, T. M., & Hausch, F. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01098-1 · Cited by 22
“Our results confirm that the ligand-binding domain of GR is the predominant interaction site for FKBPs, in line with prior studies 32 , and clearly show that FKBP51 and FKBP52 engage in extensive contacts with GR LBD .”
Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function
Seraphim, T. V., Chakafana, G., Shonhai, A., & Houry, W. A. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00605-3 · Cited by 21
Molecular chaperones in stroke-induced immunosuppression
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Multi-Omics Analysis of the Expression and Prognosis for FKBP Gene Family in Renal Cancer
Sun, Z., Qin, X., Fang, J., Tang, Y., & Fan, Y. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.697534 · Cited by 22
“FKBP5 is associated with androgen, glucocorticoid, estrogen, and mineralocorticoid receptors and acts as a negative regulator, except in the case of androgen receptors (21, 22).”
BackgroundUnique proline-rich domain regulates the chaperone function of AIPL1.
Li, J., Žoldák, G., Kriehuber, T., Soroka, J., Schmid, F., Richter, K., & Buchner, J. (2013) · Biochemistry · doi:10.1021/bi301648q · Cited by 20
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“Liganded GR replaces FKBP51 with FKBP52 to translocate into the nucleus [27, 28].”
BackgroundRole of FK506 Binding Proteins in Neurodegenerative Disorders
Chattopadhaya, S., Harikishore, A., & Yoon, H. S. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711798194441 · Cited by 20
“In the cytoplasm, FKBPs have important roles in protein stability [20-22], protein trafficking [23, 24], receptor signaling [25-27], kinase activity and maintenance of intracellular Ca 2+ homeostasis via interaction with calcium channels like the ryanodine receptor (RyR) and inositol 1,4,5-triphosphate receptor (IP3R)…”
BackgroundEvidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding
Cox, M. B., & Johnson, J. L. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7477-1_28 · Cited by 21
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“Hsp90/70 is required for the normal activity of GCRs, and FKBP52 can increase the GCR hormone-binding affinity and potentiate GCs signaling in vivo [38].”
BackgroundA Novel Decalin-Based Bicyclic Scaffold for FKBP51-Selective Ligands
Feng, X., Sippel, C., Knaup, F. H., Bracher, A., Staibano, S., Romano, M. F., & Hausch, F. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01157 · Cited by 19
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“Thus, while FKBP5 seems to block GC action by reducing receptor affinity for the ligands, FKBP4 increases its ligand affinity, allowing translocation of the receptor to the nucleus [60,64].”
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FKBPL: a marker of good prognosis in breast cancer
Nelson, L., McKeen, H. D., Marshall, A., Mulrane, L., Starczynski, J., Storr, S. J., Lanigan, F. T., Byrne, C., Arthur, K., Hegarty, S. M., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3528 · Cited by 18
“FKBP51 is another FKBP which has been shown to play a role in steroid hormone signalling, where it displays both inhibitory [47] and stimulatory [48] roles.”
Ratajczak, T. (2015) · Current Molecular Pharmacology · doi:10.2174/1874467208666150519113639 · Cited by 18
Self-citationTricyclic antidepressants target FKBP51 SUMOylation to restore glucocorticoid receptor activity
Budziñski, M. L., Sokn, C., Gobbini, R., Ugo, B., Antunica-Noguerol, M., Senin, S., Bajaj, T., Gassen, N. C., Rein, T., Schmidt, M. V., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01491-0 · Cited by 17
“Upon GC stimulation, FKBP51 is exchanged for FKBP52, which positively regulates GR activity [22, 71, 72].”
BackgroundLeMaster, D. M., Mustafi, S. M., Brecher, M. B., Zhang, J., Heroux, A., Li, H., & Hernández, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.650655 · Cited by 18
“The FK1 domain mediates the selectivity of interaction for steroid receptor binding exchange (15, 16), dynein binding (6), and inhibition of the Akt kinase (12).”
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“Among the physiological roles demonstrated for FKBPs are receptor signalling (Riggs et al., 2003), calcium homeostasis (Jayaraman et al., 1992; Cameron et al., 1995), transcription (Yang et al,. 1995), protein trafficking and stability (Shirane et al., 2003; Jinwal et al., 2010; Ahearn et al.,…”
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“For example, FKBP51 inhibits the transcriptional activity of the glucocorticoid receptor [31-33], while FKBP52 is important for promoting the transcriptional activity of this receptor [32-35].”
BackgroundPost-translational modifications and stress adaptation: the paradigm of FKBP51
Rein, T. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190332 · Cited by 15
Inactivation of ID 4 promotes a CRPC phenotype with constitutive AR activation through FKBP 52
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“The final mature complex in which the receptor is capable of high-affinity hormone binding includes heat shock protein 90 (Hsp90), the p23 cochaperone, and the 52-kDa FK506-binding protein (FKBP52, also termed FKBP4) (Cheung-Flynn et al., 2005; Riggs et al., 2003; Tranguch et al., 2005).”
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“Indeed, FKBP52 selectively potentiated hormone-dependent gene activation in Saccharomyces cereviviae by as much as 20-fold at limiting concentrations and this potentiation was blocked when FKBP51 was coexpressed (Riggs et al., 2003).”
BackgroundModulation of the Glucocorticoid Receptor Activity by Post-Translational Modifications
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“Therefore, FKBP52 is regarded as a positive regulator of GR transcriptional activity [57] and FKBP51 as a negative regulator [58].”
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Self-citationThe FKBP52 Cochaperone Acts in Synergy with β-Catenin to Potentiate Androgen Receptor Signaling
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FKBP4 regulates 5-fluorouracil sensitivity in colon cancer by controlling mitochondrial respiration
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“To address this question, we established HCT116 cells bearing the K354A mutation in the TPR domain of FKBP4 (FKBP4-K354A) (Fig S1A) that has been widely shown to abolish FKBP4/ HSP90 interaction (Cheung-Flynn et al, 2003; Riggs et al, 2003; Zong et al, 2021).”
Soto, O. B., Ramirez, C. S., Koyani, R. D., Rodriguez‐Palomares, I. A., Dirmeyer, J. R., Grajeda, B. I., Roy, S., & Cox, M. B. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30406 · Cited by 13
“52 Overall, FKBP51 has been reported to act as a negative regulator of SHR activity, as opposed to FKBP52 which positively regulates AR, GR, and PR.”
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“…2010), histone chaperone activity (Kuzuhara and Horikoshi, 2004; Nelson et al., 2006), receptor signaling (Cameron et al., 1995; Wang et al., 1996; Riggs et al., 2003), * Correspondence to: Ho Sup Yoon, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore…”
BackgroundConformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design
LeMaster, D. M., & Hernández, G. (2015) · Current Molecular Pharmacology · doi:10.2174/1874467208666150519113146 · Cited by 13
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The evolution and diversification of the Hsp90 co-chaperone system
Engler, S., & Büchner, J. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0112 · Cited by 12
Byrne, C., Henen, M. A., Belnou, M., Cantrelle, F., Kamah, A., Qi, H., Giustiniani, J., Chambraud, B., Baulieu, É.-É., Lippens, G. M., et al. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00506 · Cited by 12
The Role of HSP90 Molecular Chaperones in Depression: Potential Mechanisms
Fan, X., Sun, L., Qin, Y., Liu, Y., Wu, S., & Du, L. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04284-4 · Cited by 13
“After binding with the co-chaperone FK506 binding protein 51 (FKBP51), Hsp90 further regulates HPA axis homeostasis by regulating the activity of glucocorticoid receptors [12].”
Adipogenesis is under surveillance of Hsp90 and the high molecular weight Immunophilin FKBP51
Toneatto, J., Charó, N. L., Galigniana, N. M., & Piwien‐Pilipuk, G. (2015) · Adipocyte · doi:10.1080/21623945.2015.1049401 · Cited by 11
“FKBP51 and FKBP52 share 60% identity and 70% similarity; however the former has been so far mainly reported to be a negative regulator of steroid hormone receptors while the latter is a positive one.(51,53,55-58) When differentiation of 3T3-L1 preadipocytes is induced, it was reported that FKBP51 had a transient expre…”
BackgroundRispal, D., Henri, J., TILBEURGH, H. V., Graille, M., & Séraphin, B. (2011) · RNA · doi:10.1261/rna.2697111 · Cited by 11
“Moreover, this protein and Tpa1 copurify with the yeast nuclear pore complex (Rout et al. 2000), suggesting that they could be involved in mRNA export similarly to Dbp5, Npl3, and Gle1, which also influence translation termination efficiency (Gross et al. 2007; Bolger et al. 2008; Estrella et al.…”
BackgroundGenomic Variation, Evolvability, and the Paradox of Mental Illness
Gualtieri, C. T. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2020.593233 · Cited by 11
“One HSP, hsp90, is necessary for the glucocorticoid receptor to develop (285) and regulates receptor activity (286).”
BackgroundChaperones and ADP-Ribosylating Bacterial Toxins
Barth, H., & Ernst, K. (2016) · Springer eBooks · doi:10.1007/978-94-007-6725-6_7-1 · Cited by 10
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A patent review of anticancer glucocorticoid receptor modulators (2014-present)
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“exposes nuclear translocation signals [32], binding to nucleo-”
BackgroundAlternative splicing of FKBP5 gene exerts control over T lymphocyte expansion
Marrone, L., D’Agostino, M., Cesaro, E., Giacomo, V. D., Urzini, S., Romano, M. F., & Romano, S. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30364 · Cited by 9
Genomic and non-genomic effects of glucocorticoids in respiratory diseases
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FK506 binding protein 51: Its role in the adipose organ and beyond
Galigniana, N. M., Ruiz, M. C., & Piwien‐Pilipuk, G. (2022) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30351 · Cited by 11
“They correspond to: citation number 26 and it has to be added ‐ Storer CL, DickeyCA, Galigniana MG, ReinT, Cox MB. 2011.”
Impact of FKBP52 on cell proliferation and hormone‐dependent cancers
Hanaki, S., & Shimada, M. (2023) · Cancer Science · doi:10.1111/cas.15811 · Cited by 7
Ejiohuo, O., Bajia, D., Pawlak, J., & Szczepankiewicz, A. (2025) · PLoS ONE · doi:10.1371/journal.pone.0320017 · Cited by 9
“The FK1 domain of FKBP proteins is associated with its regulatory function for glucocorticoid receptor (GR) [84].”
Thirumoorthy, C., Rekha, R., Deepa, M., Ram, U., Shalu, D., Venkatesan, U., Srikumar, B. N., Anjana, R. M., Balasubramanyam, M., Mohan, V., et al. (2025) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2025.107431 · Cited by 8
Surkin, P. N., Brenhouse, H. C., Terrence Deak, B., Liberman, A. C., & Lasaga, M. (2018) · Journal of Neuroendocrinology · doi:10.1111/jne.12602 · Cited by 8
“The fine-tuning for GR nuclear translocation is mediated by these immunophilins since FKBP52 promotes nucleus migration favoring GR transcriptional activity and FKBP51 prevents it [59], [60].”
BackgroundHu, X., Liu, L., Wang, Z., Sun, Y., Li, Z., Zhou, G., Yue, K., Wang, L., Lian, B., Lü, G., et al. (2023) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2023.110697 · Cited by 8
Rajan, S. S., Austin, D., Harikishore, A., Nguyen, Q. T., Baek, K., & Yoon, H. S. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24487 · Cited by 8
Protective role of FKBP51 in calcium entry‐induced endothelial barrier disruption
Hamilton, C. L., Kadeba, P. I., Vasauskas, A. A., Solodushko, V., McClinton, A. K., ALEXEYEV, M. F., Scammell, J. G., & Cioffi, D. L. (2017) · Pulmonary Circulation · doi:10.1177/2045893217749987 · Cited by 8
“FKBP51 and FKBP52 are members of the FK506-binding protein immunophilin family that are best known for their roles in steroid receptor signaling, where they have opposing effects on receptor function.(11,12) Whereas FKBP52 potentiates steroid receptor activation, FKBP51 inhibits activation.”
BackgroundFunctions of the Hsp90-Binding FKBP Immunophilins
Cox, M. B., & Smith, D. F. (2007) · Springer eBooks · doi:10.1007/978-0-387-49310-7_2 · Cited by 7
Self-citationRios, E. I., Hunsberger, I. L., & Johnson, J. L. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1325590 · Cited by 7
Cucuzza, L. S., BIOLATTI, B., Scaglione, F. E., & Cannizzo, F. T. (2017) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2017.08.001 · Cited by 7
Gao, Y., Elamin, E., Zhou, R., Yan, H., Liu, S., Hu, S., Dong, J., Wei, M., Sun, L., & Zhao, Y. (2018) · Oncology Letters · doi:10.3892/ol.2018.9517 · Cited by 7
“FKBP51 interacts with glucocorticoid, androgen, estrogen, progestin and mineralocorticoid receptors (2-7) through a number of components of the molecular chaperone machinery, including heat shock protein 90.”
“Tuning” the ATPase Activity of Hsp90
Prodromou, C., & Morgan, R. M. L. (2015) · Springer eBooks · doi:10.1007/978-3-319-24780-9_23 · Cited by 7
SUMO conjugation as regulator of the glucocorticoid receptor-FKBP51 cellular response to stress
Liberman, A. C., Budziñski, M. L., Sokn, C., Gobbini, R. P., Ugo, M. B., & ARZT, E. S. (2019) · Steroids · doi:10.1016/j.steroids.2019.108520 · Cited by 7
Anderson, J. S., Mustafi, S. M., Hernández, G., & LeMaster, D. M. (2014) · Biophysical Chemistry · doi:10.1016/j.bpc.2014.06.004 · Cited by 6
Harris, D. C., Garcia, Y. A., Samaniego, C., Rowlett, V. W., Ortiz, N. R., Payan, A. N., Maehigashi, T., & Cox, M. B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215346 · Cited by 6
“We propose that the HsFKBP52 proline-rich loop, also referred to as the β 4– β 5 loop, via the open conformation that exposes the hydrophobic notch, forms a specific contact with the receptor ligand-binding domain (LBD).”
BackgroundMethodResultInfluentialElevated FKBP52 expression indicates a poor outcome in patients with breast cancer
Hong, C., Li, T., Zhang, F., Wu, X., Chen, X., Cui, X., Zhang, G., & Cui, Y. (2017) · Oncology Letters · doi:10.3892/ol.2017.6828 · Cited by 6
Molecular determinants ofDrosophilaimmunophilin FKBP39 nuclear localization
Orłowski, M., Popławska, K., Pieprzyk, J., Szczygieł-Sommer, A., Więch, A., Zarębski, M., Tarczewska, A., Dobrucki, J. W., & Ożyhar, A. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0251 · Cited by 6
“The immunophilins FKBP51 and FKBP52 were found to act as co-chaperones of Hsp90 during steroid receptor signaling (Riggs et al., 2003; Galigniana et al., 2012; Quinta aPresent address: Polpharma Biologics, Gdańsk Science and Technology Park, 80-172 Gdańsk, Poland bPresent address: EMBL Hamburg…”
BackgroundHsp90: From Dispensable Heat Shock Protein to Global Player
Richter, K., Meinlschmidt, B., & Büchner, J. (2005) · Wiley eBooks · doi:10.1002/9783527619498.ch56 · Cited by 6
Molecular mechanism of PINK1 regulation by the Hsp90 machinery
Tian, X., Su, J., Wang, Z., Liu, T., Xiong, H., Sun, S., Mei, K., & Sui, S. (2025) · Nature Communications · doi:10.1038/s41467-025-65859-w · Cited by 6
“The FK1 domain primarily exhibits peptidyl-prolyl isomerase (PPIase) activity, allowing it to facilitate the cis-trans isomerization of peptide bonds preceding proline residues in substrate proteins 27 , thereby ensuring proper protein folding and function 55 .”
Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function
Backe, S. J., Mollapour, M., & Woodford, M. R. (2023) · Essays in Biochemistry · doi:10.1042/ebc20220224 · Cited by 5
Crystal structure and conformational flexibility of the unligated FK506-binding protein FKBP12.6
Chen, H., Mustafi, S. M., LeMaster, D. M., Li, Z., Heroux, A., Li, H., & Hernández, G. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004713032112 · Cited by 5
Noncanonical Mechanisms to Regulate Nuclear Receptor Signaling
Sadana, P. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.72 · Cited by 6
FKBP51 functions in the regulation of circadian rhythm and Alzheimer's disease
Johnson, J. L. (2025) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2025.02.002 · Cited by 4
Obrenovic, B., Godinić, D., Du, G., Khudaykulov, A., & Gan, H. (2024) · Behavioral Sciences · doi:10.3390/bs14080648 · Cited by 9
“Inhibitory control deficits were previously found to be associated with internalizing [58] and externalizing behavioral problems [59].”
BackgroundAraki, T., Kawamura, M., Tanaka, K., Okita, Y., Fujikawa, H., Uchida, K., Toiyama, Y., Inoue, Y., Mohri, Y., & Kusunoki, M. (2015) · Digestive Diseases and Sciences · doi:10.1007/s10620-015-3528-9 · Cited by 4
“As a result, overexpression of FKBP51 decreases receptor regulation by FKBP52 [9].”
BackgroundInfluentialRole of the Hsp90-Immunophilin Heterocomplex in Cancer Biology
Leo, S. A. D., Zgajnar, N. R., Mazaira, G. I., Erlejman, A. G., & Galigniana, M. D. (2019) · Current Cancer Therapy Reviews · doi:10.2174/1573394715666190102120801 · Cited by 4
High-yield expression and purification of the Hsp90-associated p23, FKBP52, HOP and SGTα proteins
Hildenbrand, Z. L., Molugu, S. K., Paul, A., Avila, G. A., Herrera, N., Xiao, C., Cox, M. B., & Bernal, R. A. (2010) · Journal of Chromatography B · doi:10.1016/j.jchromb.2010.08.016 · Cited by 4
Balsiger, H. A., & Cox, M. B. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-575-0_8 · Cited by 4
Navigating glucocorticoid resistance: From GR isoforms to nuclear condensates
Wang, C., Zhong, Y., Tang, M., He, X., Xu, S., & Zhang, J. (2025) · Cell investigation. · doi:10.1016/j.clnves.2025.100059 · Cited by 3
Glucocorticoid receptor signaling: crosstalk with inflammation
Zhan, X., Song, B., Xu, S., & Zhou, H. (2026) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2025.2605579 · Cited by 3
“…by FKBP52 (encoded by Fkbp4 ), causing conformational alterations in GR that reveal two NlS, thus facilitating GR’s movement into the nucleus [83]. the understanding of GR nuclear translocation has shifted from the notion that GR simply detaches from cytoplasmic chaperones upon ligand…”
The animal and cell models that uncovered FKBP51 as a regulator of glucocorticoid receptor function
Scammell, J. G. (2023) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30375 · Cited by 3
Wang, C., Zhong, Y., Xu, S., Cai, W., Zhao, J., Mao, J., Jin, H., Ouyang, C., Shi, Y., Chan, W. C., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101270 · Cited by 4
Functions of the Hsp90-Binding FKBP Immunophilins
Ortiz, N. R., Guy, N. C., Garcia, Y. A., Sivils, J. C., Galigniana, M. D., & Cox, M. B. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-14740-1_2 · Cited by 3
The transportosome system as a model for the retrotransport of soluble proteins
Mazaira, G. I., Erlejman, A. G., Zgajnar, N. R., Piwien‐Pilipuk, G., & Galigniana, M. D. (2023) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2023.112047 · Cited by 3
Liu, L., Cheng, J., Wei, F., Pang, L., Zhi, Z., Yang, W., & Tan, W. (2021) · Organogenesis · doi:10.1080/15476278.2020.1860424 · Cited by 3
“In addition, the study found that the expression of FKBP52 in ectopic tissue of endometriosis patients decreased significantly and it was related to the growth of endometriosis lesions, which inhibited the binding ability of PR-A and progesterone by affecting the binding ability of PR-A and HSP90, and made the functio…”
BackgroundRole of FKBP51 and FKBP52 in glucocorticoid receptor regulated metabolism
Warrier, M. (2008) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 3
Oh, D., Choi, M., Han, D. M. R., Chai, Y. G., & Choi, J. (2014) · Neuroreport · doi:10.1097/wnr.0000000000000284 · Cited by 3
Ruqaiyah1, 2. (2020) · Indian Journal of Forensic Medicine & Toxicology · doi:10.37506/ijfmt.v14i4.12153 · Cited by 3
Photoreceptor-dependent signaling in plant responses to thermomorphogenesis and heat stress
Zhang, Y., Wu, L., Yuan, K., & Yu, Y. (2025) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2025.110202 · Cited by 2
Anderson, J. S., LeMaster, D. M., & Hernández, G. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105159 · Cited by 2
“All these interactions are preserved in crystal structures of the evolutionarily related FKBP12 (PDB code: 2PPN (46)) and FKBP52 FK1 domain (PDB code: 4LAV (12)).”
InfluentialWang, X., Tang, H., Jian, L. U., & Xia, Z. (2010) · Chinese Medical Journal · doi:10.3760/cma.j.issn.0366-6999.2010.13.030 · Cited by 2
FKBP Co-Chaperones in Steroid Receptor Complexes
Cheung‐Flynn, J., Place, S. P., Cox, M. B., Prapapanich, V., & Smith, D. F. (2007) · Springer eBooks · doi:10.1007/978-0-387-39717-7_12 · Cited by 2
Self-citationOsFKBP1 interacts with phytochrome B in rice
Gu, S., Zhang, F., & Wu, N. (2009) · Progress in Natural Science Materials International · doi:10.1016/j.pnsc.2009.05.001 · Cited by 2
“In mammals, FKBP52 promotes translocation of the glucocorticoid receptor to the nucleus [42–44].”
BackgroundZhang, Y., Xia, G., Sheng, L., Chen, M., Hu, C., Ye, Y., Yue, X., Chen, S., OuYang, W., & Xia, Z. (2022) · Plant Cell Reports · doi:10.1007/s00299-022-02910-w · Cited by 2
Genomic and non-genomic effects of glucocorticoids
Тодосенко, Н. М., Koroleva, Y. A., Геннадьевна, Х. О., Yurova, K. A., & Litvinova, L. S. (2017) · Genes and Cells · doi:10.23868/gc120636 · Cited by 2
Metadata
- Authors
- Riggs, D. L., Roberts, P. J., Chirillo, S. C., Cheung‐Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Picard, D., & Smith, D. F.
- Affiliations
- Mayo Clinic (US)
- The University of Western Australia (AU)
- Northwestern University (US)
- University of Geneva (CH)
- Corresponding author
- Smith, David F.
- Venue
- The EMBO Journal
- Published
- 2003-03-03
- Volume
- 22
- Issue
- 5
- Pages
- 1158-1167
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC150341
- OpenAlex
- W2075431153
- Semantic Scholar
- 1ac04c1350d5c46f954ac9ade4bc83458748b0ac
- Cited by
- 353
- References
- 58
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 6 · 2023: 19 · 2022: 13 · 2021: 16 · 2020: 13 · 2019: 16 · 2018: 9 · 2017: 14 · 2016: 15 · 2015: 21 · 2014: 16 · 2013: 18 · 2012: 16
- FWCI
- 6.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Science Foundation (0079249)
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (DK44923, R01DK044923, R01DK048218)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Keywords
- FKBP52, HSP90, immunophilins, glucocorticoid receptor, glucocorticoid signaling, peptidylprolyl isomerase, FKBP51, hormone binding affinity, Saccharomyces cerevisiae, protein phosphatase 5
- MeSH terms
- Animals, Dose-Response Relationship, Drug, Gene Expression Regulation, Glucocorticoids, Humans, Models, Molecular, Protein Binding, Protein Conformation, Receptors, Glucocorticoid, Saccharomyces cerevisiae, Signal Transduction, Transcriptional Activation, Genes, Reporter, Molecular Chaperones, HSP90 Heat-Shock Proteins, Peptidylprolyl Isomerase, Tacrolimus Binding Proteins
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