Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore
Open accessAbstract
In the absence of hormone, corticosteroid receptors such as GR (glucocorticoid receptor) and (mineralocorticoid receptor) are primarily located in the cytoplasm. Upon steroid-binding, they rapidly accumulate in the nucleus. Regardless of their primary location, these receptors and many other nuclear factors undergo a constant and dynamic nucleocytoplasmic shuttling. All members of the steroid receptor family are known to form large oligomeric structures with the heat-shock proteins of 90-kDa (hsp90) and 70-kDa (hsp70), the small acidic protein p23, and a tetratricopeptide repeat (TPR) -domain protein such as FK506-binding proteins (FKBPs), cyclophilins (CyPs) or the serine/threonine protein phosphatase 5 (PP5). It has always been stated that the dissociation of the chaperone heterocomplex (a process normally referred to as receptor "transformation") is the first step that permits the nuclear import of steroid receptors. However the experimental evidence is consistent with a model where the chaperone machinery is required for the retrotransport of the receptor through the cytoplasm and also facilitates the passage through the nuclear pore. Recent evidence indicates that the hsp90-based chaperone system also interacts with structures of the nuclear pore such as importin β and the integral nuclear pore glycoprotein Nup62 facilitating the passage of the untransformed receptor through the nuclear pore.
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FKBP52 stabilizes ligand-bound GR, resulting in enhanced ligand affinity, and facilitates rapid GR nuclear translocation on dynein, allowing GR to proceed with dimerization and transcription activation.
“FKBP52 stabilizes ligand-bound GR, resulting in enhanced ligand affinity, and facilitates rapid GR nuclear translocation on dynein22,24,25,65, allowing GR to proceed with dimerization and transcription activation.”
From Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor (2023) · cites this paper as [65]
SHRs are not confined to any particular cell compartment and shuttle continuously between cytoplasm and nucleus.
“Regardless of their primary localization, these receptors are not confined to any particular cell compartment and shuttle continuously between cytoplasm and nucleus [16, 17].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [17]
The rapid, hsp90•FKBP-dependent movement of steroid receptors requires cytoskeletal tracts, with tubulin physically linked to the receptor•hsp90•FKBP52•motor protein complex.
“The rapid, hsp90•FKBP-dependent movement of steroid receptors requires cytoskeletal tracts, tubulin being physically linked to the receptor•hsp90•FKBP52•motor protein complex [17, 24].”
From FKBP51 and FKBP52 in signaling and disease (2011) · cites this paper as [17]
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“FKBP52 stabilizes ligand-bound GR, resulting in enhanced ligand affinity, and facilitates rapid GR nuclear translocation on dynein 22,24,25,65 , allowing GR to proceed with dimerization and transcription activation.”
BackgroundBracher, 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
- Authors
- Galigniana, M. D., Echeverría, P. C., Erlejman, A. G., & Piwien-Pilipuk, G.
- Affiliations
- Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
- University of Geneva (CH)
- Universidad de Buenos Aires (AR)
- Corresponding author
- Galigniana, Mario D.
- Venue
- Nucleus
- Publisher
- Informa UK Limited
- Published
- 2010-07
- Volume
- 1
- Issue
- 4
- Pages
- 299-308
- ISSN
- 1949-1034 (ISSN-L)
- 1949-1042
- PMC
- PMC2990191
- OpenAlex
- W1995288330
- Semantic Scholar
- 853928fd1ce24cfe308ae4ec0d14d204fecb3f04
- Cited by
- 114
- References
- 76
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 1 · 2023: 12 · 2022: 4 · 2021: 13 · 2020: 4 · 2019: 11 · 2018: 9 · 2017: 2 · 2016: 7 · 2015: 8 · 2014: 11 · 2013: 8 · 2012: 4
- FWCI
- 3.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Nucleus (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
- Funders
- National Institutes of Health (5r03tw007162-03)
- Fogarty International Center (R03-TW007162, R03TW008143)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Keywords
- steroid hormone receptors, glucocorticoid receptor, mineralocorticoid receptor, molecular chaperones, HSP90, HSP70, p23, tetratricopeptide repeat proteins, FKBP, cyclophilin, protein phosphatase 5, nucleocytoplasmic shuttling, nuclear import, nuclear pores, importin beta, Nup62
- MeSH terms
- Cell Nucleus, Models, Molecular, Nuclear Proteins, Phosphoprotein Phosphatases, Receptors, Steroid, Molecular Chaperones, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Immunophilins, Active Transport, Cell Nucleus, Cyclophilins, Tacrolimus Binding Proteins, Nuclear Pore, beta Karyopherins
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