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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FKBP52 binding to Hsp90 is required for regulation of AR activity.
“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]
The ‘Selectivity of FKBP52 for GR’ section says FKBP52 did not enhance androgen receptor activity in yeast. The Hsp90-binding requirement reported in ‘Mechanism of FKBP52 action’ applies to potentiation of glucocorticoid receptor (GR) activity, not AR activity. (LLM, conf=0.90)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredFKBP52 enhances GR, PR, and AR responsiveness to cognate hormone.
“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]
The paper supports enhanced GR responsiveness, but its “Selectivity of FKBP52 for GR” section explicitly reports that FKBP52 did not enhance androgen- or progesterone-receptor reporter activity. That contradicts the claim that it enhances AR and PR responsiveness as well. (LLM, conf=0.90)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredFKBP52 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 [7]
The Discussion reports that FKBP52 boosts GR activity. But “Selectivity of FKBP52 for GR” states that FKBP52 did not enhance androgen- or progesterone-receptor reporter activity in the yeast tests. The paper supports functional interaction with GR, not the claimed functional effects on all three receptors. (LLM, conf=0.88)
Experimental — accuracy not yet measuredFKBP51 inhibits GR ligand binding, nuclear translocation and transcriptional activity, while FKBP52 potentiates each of these activities.
“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]
The Discussion reports that FKBP52 raises GR hormone-binding affinity and boosts reporter activity. The section on immunophilin influence says FKBP51 was known to inhibit GR activity in mammalian systems, but this study did not observe that inhibition in yeast; it found that FKBP51 blocked FKBP52-mediated potentiation. The Mechanism section discusses nuclear transport as a proposal from other researchers, not as a demonstrated effect of either protein here, so the claim about nuclear translocation is unsupported by this paper. (LLM, conf=0.87)
Experimental — accuracy not yet measuredUnlike FKBP52, FKBP51 does not enhance GR ligand binding in vitro.
“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]
The “FKBP52 and GR hormone binding” section reports greater GR hormone binding in yeast cells expressing FKBP52 than in cells expressing FKBP51. The assays used intact cells, however, so this paper does not establish the claim specifically for in vitro ligand binding. Page numbers are unavailable in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measured
The relative concentrations of FKBP51 and FKBP52 in the cell dictate the level of GR activity in vivo.
“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]
The Discussion reports that FKBP52 boosts GR reporter activity in yeast and that FKBP51 blocks this potentiation. This supports a role for the two proteins in GR activity, but the paper does not establish that their relative cellular concentrations dictate GR activity generally; its direct tests use a yeast model. (LLM, conf=0.84)
Experimental — accuracy not yet measuredCo-expression of FKBP52 (K354A), which completely lacks Hsp90 binding, with β-catenin (S33A) resulted in 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.
“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]
FKBP51 does not potentiate GR ligand binding in any of these conditions, unlike FKBP52, recapitulating in vivo findings.
“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]
FKBP52 potentiates GR ligand binding affinity beyond the minimal chaperone mixture, consistent with reports in vivo.
“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]
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 [5]
FKBP52 regulation has been localized to the receptor ligand binding domain (LBD), suggesting that the FK1 interaction partner is the receptor LBD.
“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]
The FK1 domain facilitates binding to FK506, confers PPIase activity, and is the primary regulatory domain for SHRs.
“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]
FKBPs compete for binding to the SHR complex, and overexpression of FKBP51 decreases receptor regulation by FKBP52.
“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]
The FK1 domain is critical for receptor potentiation by FKBP52, but its enzymatic activity is not required for this potentiation.
“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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Self-citationFK506-Binding Proteins and Their Diverse Functions
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“Transfection of FKBP52 into Saccharomyces cerevisiae (21) or overexpression in mammalian cells (22) caused potentiation of GR-mediated reporter gene expression that correlated with an increase in GR hormone-binding function.”
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“Yet, it is clear that the PPIase domain (rather than catalytic activity) is critical to FKBP52 actions on GR and PR (Riggs et al., 2003; Tranguch et al., 2005; Wochnik et al., 2005).”
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Multidomain Peptidyl Prolyl cis/trans Isomerases
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NF-κB Transcriptional Activity Is Modulated by FK506-binding Proteins FKBP51 and FKBP52
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Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52
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“In contrast to FKBP51, the better-studied FKBP52 serves to promote the molecular activities of both GR and AR [23,27,28].”
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Fluorescent Probes to Characterise FK506‐Binding Proteins
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Self-citationStructure and function of Hip, an attenuator of the Hsp70 chaperone cycle
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The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation
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Self-citation
- 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 › Genetics › 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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