Cited by 423Heat shock proteins researchFungal and yeast genetics researchProtein Structure and Dynamics

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Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase

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Nathan, Debra F., Lindquist, Susan·1995·Molecular and Cellular Biology

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Abstract

Hsp90 is a protein chaperone whose functions are focused on a specific set of target proteins. The nature of Hsp90's interactions with these proteins is poorly understood. To provide tools for examining these interactions, we have isolated eight broadly distributed temperature-sensitive (ts) point mutations in the Hsp90 gene (HSP82) of Saccharomyces cerevisiae. The mutants fall into two distinct classes. One has a classic ts phenotype, with nearly wild-type activity at 25 degrees C and a precipitous loss of function at 34 degrees C. The remaining seven mutants, in contrast, cause a general reduction in Hsp90 function and are ts because they do not provide the high level of function required for growth at high temperatures. The effects of these mutants on two target proteins, a transcription factor (glucocorticoid receptor) and a tyrosine kinase (pp60v-src), provided several insights on Hsp90 function. First, Hsp90 is not only required to help the glucocorticoid receptor achieve a hormone-activable state, it is continuously required to maintain that state. Second, Hsp90's function in the maturation of pp60v-src involves separable roles in protein accumulation and kinase activation. Thus, Hsp90 is an integral component of both the steroid receptor and kinase signaling pathways. Finally, all eight point mutants affect the activation of both the glucocorticoid receptor and pp60v-src, indicating that Hsp90 promotes the activity of these very different target proteins through common mechanisms.

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10.1128/mcb.9.9.3919-3930.1989 · DOI · Paper page
10.1128/mcb.13.9.5290-5300.1993 · DOI
Parsell, D. A., and S. Lindquist. 1994. Heat shock proteins and stress tolerance, p. 457–494. In R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.

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“pendent manner when ectopically expressed in yeast (Nathan and Lindquist, 1995).”
Background
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Method
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Background
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Self-citation
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Background
Hsp90 and phosphorylation of the Slt2(Mpk1) MAP kinase activation loop are essential for catalytic, but not non-catalytic, Slt2-mediated transcription in yeast
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Background
The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae
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“cerevisiae mutants that are temperaturesensitive (ts) due to point mutations in Hsp82, their sole form of Hsp90 (Nathan and Lindquist, 1995).”
Influential
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BackgroundInfluential
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Background
GR chaperone cycle mechanism revealed by cryo-EM: inactivation of GR by GR:Hsp90:Hsp70:Hop client-loading complex
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Brenner, J. C., Zirden, L. C., Buzuk, L., Almeida‐Hernández, Y., Radzuweit, L., Diamantino, J., Kaschani, F., Kaiser, M., Sánchez‐García, E., Poepsel, S., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01619-0 · Cited by 7
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“It participates in regulating the activity of signalling proteins, such as the steroid receptors, and the kinases Ras, Raf and pp60v2svc [37–43].”
Background
Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions
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Background
Ribosome‐associated quality control mediates degradation of the premature translation termination product Orf1p of ODC antizyme mRNA
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“yAT01 P82a W303–1a hsc82::LEU2 hsp82::LEU2 HIS3-GPD-HSP82a [31]”
BackgroundInfluential
Molecular Control of Endothelial Derived Nitric Oxide
Gratton, J., Fontana, J. T., & Sessa, W. C. (2000) · Elsevier eBooks · doi:10.1016/b978-012370420-7/50010-1 · Cited by 5
An Updated Review on KRAS Mutation in Lung Cancer (NSCLC) and Its Effects on Human Health
Ghosh, S., Bhuniya, T., Dey, A., Koley, M., Roy, P., Bera, A., Gol, D., Chowdhury, A., Chowdhury, R., & Sen, S. (2023) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-023-04748-8 · Cited by 5
“Additionally, mutant oncoproteins, such as the epidermal growth factor receptor (EGFR), may depend on Hsp90 chaperones more frequently than their wild-type counterparts, which makes Hsp90 an even more attractive therapeutic target for malignancies characterized by such mutations [33–36].”
Yeast-Based Reporter Assays for the Functional Characterization of Cochaperone Interactions with Steroid Hormone Receptors
Balsiger, H. A., & Cox, M. B. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-575-0_8 · Cited by 4
Identifying functional interactions with molecular chaperones
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Development of a quantitative RT-PCR system for the specific detection of human heat shock mRNA expression
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A systematic survey of an intragenic epistatic landscapePreprint
Bank, C., Hietpas, R. T., Jensen, J. D., & Bolon, D. N. A. (2014) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/010645 · Cited by 6
“Briefly, mutants were encoded on p417GPD, a plasmid/promoter system that closely matches the endogenous expression of Hsp90 (Nathan and Lindquist 1995).”
Background
Hsp90: A means to an end
Whalen, K. M., & Freeman, B. (2026) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2026.100190 · Cited by 3
“3,50 For instance, an allele (E431K) was isolated that did not support hormone binding by the glucocorticoid receptor but was near wild type for three highly related aporeceptors (mineralocorticoid, progesterone, and estrogen receptors).”
Indispensable Role of Protein Turnover in Autophagy, Apoptosis and Ubiquitination Pathways
Abosheasha, M. A., Khalik, E. A. M. A. E., & El‐Gowily, A. H. (2020) · Heat shock proteins · doi:10.1007/7515_2020_31 · Cited by 3
Histidine Kinases
Yang, W. (2003) · Elsevier eBooks · doi:10.1016/b978-012372484-7/50012-6 · Cited by 3
Hsp104–Hsp70–Hsp110 chaperones disintegrate kinase aggregates formed upon stress in Saccharomyces cerevisiae
Bhattacharjee, P., & Mandal, A. K. (2025) · FEBS Letters · doi:10.1002/1873-3468.70174 · Cited by 2
“The details of yeast strains used in this study are listed in Table S1 [15].”
Chronic Obstructive Pulmonary Disease – Chaperonopathology
Cherneva, R. V., Петрова, Д., & Georgiev, O. B. (2012) · InTech eBooks · doi:10.5772/30389 · Cited by 2
Heat Shock Protein 90 in Severe Trauma
Zhao, Y., & Zhou, Y.-G. (2019) · Heat shock proteins · doi:10.1007/978-3-030-23158-3_24 · Cited by 2
Inhibitors of the Hsp90 C-terminus
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Investigating the influence of environment on the evolution of Hsp90 using comprehensive fitness maps [preprint]
Flynn, J. M., Rossouw, A., Cote-Hammarlof, P. A., Fragata, I., Mavor, D., Hollins, C., Bank, C., & Bolon, D. N. A. (2019) · eScholarship@UMassChan · Cited by 2
Dominant negative mutations in yeast Hsp90 indicate triage decision mechanism targeting client proteins for degradation
Flynn, J. M., Joyce, M. E., & Bolon, D. N. A. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-07-0309 · Cited by 8
A novel Hsp90 phospho-switch modulates virulence in the major human fungal pathogen Candida albicansPreprint
Alaalm, L., Crunden, J. L., Butcher, M. C., Obst, U., Whealy, R. N., Williamson, C. E., O’Brien, H., Schaffitzel, C., Ramage, G., & Diezmann, S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.23.309831 · Cited by 2
HSP90 Co-Chaperones in Saccharomyces Cerevisiae
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Endogenous Substrates of the Euglena Chloroplast Chaperonin 60 at Permissive and Bleaching Temperatures
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Trafficking and Quality Control of Inward-Rectifying Potassium Channels in the Model Eukaryote Saccharomyces cerevisiae
Mackie, T. D. (2018) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1
Insights into the Allosteric Regulation of Human Hsp90 Revealed by NMR Spectroscopy
Goričan, T., & Grdadolnik, S. G. (2024) · Biomolecules · doi:10.3390/biom15010037 · Cited by 1
Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation
Wan, C., Zhu, L., Wang, S., Zhang, X., Zhao, J., Qu, X., & Huang, C. (2026) · Nature Communications · doi:10.1038/s41467-026-73400-w · Cited by 1
“Among them, T115 and T36 in human Hsp90 α , or their equivalent residues in other orthologs, have attracted particular attention due to their strong effects on temperature-sensitivity viability 23 , in vivo Hsp90 function 24 – 29 , and pharmacologic response in cancer cells 28 .”
Understanding of ATP-lid conformational dynamics in the N-terminal domain of Hsp90 and its mutants by use of a computational biochemistry approach
Gohda, K. (2025) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2025.2487202 · Cited by 1
“Mutants in the lid segment that affect the ATP hydrolytic activity are known among the identified Hsp90 mutants (Nathan & Lindquist, 1995; Prodromou et al., 2000; Reidy & Masison, 2020; Richter et al., 2002; Siligardi et al., 2004).”
Functional Protein Interactions in Steroid Receptor-Chaperone Complexes
Ratajczak, T., Rudi, K., Cluning, C., & Bryan, K. R. (2012) · InTech eBooks · doi:10.5772/38339 · Cited by 1
Determination of Hsp90 Activity Through Activation of Glucocorticoid Receptors in Yeast
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Hsp90 Is a Pivotal Player in Retinal Disease and Cancer
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“Lindquist (Lindquist and Kim, 1996; Nathan and Lindquist, 1995)), YEp434-A4 (SSA4), YEp351SSA2, YCp50-GAL1-SSA1, pZJHSE2-137 containing an HSE, HSE2 from SSA1 promoter fused to LacZ (kind gifts from E.”
Background
Human HSP90 isoforms: Preparation for monoclonal antibodies and expression in human salivary gland adenocarcinoma cells.
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“Among other chaperones at large, the ATP-driven Hsp90 is unique in acting in the late stages of folding on near-native states of its many ‘client’ proteins 1 .”
The Role of Molecular Chaperones in the ER Associated Degradation of the Cystic Fibrosis Transmembrane Conductance Regulator in the Budding Yeast S. cerevisiae
Youker, R. T. (2006) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1
Biochemical analysis of proteins in the telomere maintenance pathway
DeZwaan, D. C. (2011) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)
The Role of Molecular Chaperones in Yeast Cell Wall Integrity and Identification of Chaperone Modulators that Interfere with Simian Virus 40 Replication
Wright, C. M. (2007) · D-Scholarship@Pitt (University of Pittsburgh)
Inhibition of Hsp90 in Streptomyces coelicolor
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Glucocorticoid Resistance and Hypersensitivity
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The Contribution Of Molecular Chaperones To The ER-Associated Degradation Of Apolipoprotein B In Both Yeast And Mammalian Systems
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The Molecular Chaperone Hsp90 is required for Actin Dynamics during Sperm Individualization in Drosophila
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Associate Editor: D. Shugar The 90-kDa Molecular Chaperone Family: Structure, Function, and Clinical Applications. A Comprehensive Review
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Experimental Illumination of Comprehensive Fitness Landscapes: A Dissertation
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Uncovering aR egion of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast
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Authors: Nathan, D. F., & Lindquist, S.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Lindquist, Susan
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1995-07
Volume: 15
Issue: 7
Pages: 3917-3925
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.15.7.3917
PMC: PMC230631
OpenAlex: W2101287778
Cited by: 423
References: 56
Citations by year: 2026: 6 · 2025: 4 · 2024: 8 · 2023: 7 · 2022: 7 · 2021: 12 · 2020: 14 · 2019: 14 · 2018: 9 · 2017: 8 · 2016: 11 · 2015: 5 · 2014: 14 · 2013: 11 · 2012: 15
FWCI: 9.79
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Howard Hughes Medical Institute
National Institutes of Health (5f32gm014745-03)
National Institute of General Medical Sciences (GM14745-02)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: HSP90, temperature-sensitive mutants, glucocorticoid receptor, pp60v-src, tyrosine kinase, steroid receptor signaling, kinase activation, Saccharomyces cerevisiae
MeSH terms: DNA Mutational Analysis, Hot Temperature, Heat-Shock Proteins, Phenotype, Protein Binding, Receptors, Glucocorticoid, Saccharomyces cerevisiae, Oncogene Protein pp60(v-src), Point Mutation, HSP90 Heat-Shock Proteins, Saccharomyces cerevisiae Proteins

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Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase

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