Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.

Imai, Jun; Yahara, Ichiro

doi:10.1128/mcb.20.24.9262-9270.2000

Cited by 123Heat shock proteins researchFungal and yeast genetics researchPlant Stress Responses and Tolerance

Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.

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Imai, Jun, Yahara, Ichiro·2000·Molecular and Cellular Biology

DOI 10.1128/mcb.20.24.9262-9270.2000PMC PMC102183

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Abstract

The role of HSP90 in stress tolerance was investigated in Saccharomyces cerevisiae. Cells showing 20-fold overexpression of Hsc82, an HSP90 homologue in yeast, were hypersensitive to high-NaCl or H-LiCl stresses. Hsc82-overexpressing cells appeared similar to calcineurin-defective cells in salt sensitivity and showed reduced levels of calcineurin-dependent gene expression. Co-overexpression of Cna2, the catalytic subunit of calcineurin, suppressed the hypersensitivity. Cna2 and Hsc82 coimmunoprecipitated from control cells grown under normal conditions but not from stressed cells. In contrast, coimmunoprecipitation was detected with Hsc82-overexpressing cells even after exposure to stresses. Cna2 immune complexes from stressed control cells showed a significant level of calcineurin activity, whereas those from stressed Hsc82-overexpressing cells did not. Treatment of extracts from Hsc82-overexpressing cells with Ca(2+)-calmodulin increased the calcineurin activity associated with Cna2 immune complexes. Geldanamycin, an inhibitor of HSP90 abolished the coimmunoprecipitation but did not activate calcineurin. When the expression level of Hsc82 decreased to below 30% of the normal level, cells also became hypersensitive to salt stress. In these cells, the amount of Cna2 was reduced, likely as a result of degradation. The present results showed that Hsc82 binds to and stabilizes Cna2 and that dissociation of Cna2 from Hsc82 is necessary for its activation.

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Hsp90 stabilizes the catalytic subunit of calcineurin in both S. cerevisiae and C. albicans, thereby enabling calcineurin-dependent responses to drug-induced cellular stress.
“Hsp90 stabilizes the catalytic subunit of calcineurin in both S. cerevisiae and C. albicans [41], [91], thereby enabling calcineurin-dependent responses to drug-induced cellular stress [3], [92].”
From Global Analysis of the Evolution and Mechanism of Echinocandin Resistance in Candida glabrata (2012) · cites this paper as [91]
The Abstract reports that Hsc82, an Hsp90 homologue, binds and stabilizes the calcineurin catalytic subunit Cna2 in S. cerevisiae. The paper does not establish this finding in C. albicans. In the printed sentence, the separate claim about drug-induced stress carries other citations, so it is not attributed to this source. (LLM, conf=0.88)
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In S. cerevisiae, Hsp90 physically interacts with the catalytic subunit of calcineurin, keeping it stable and poised for activation.
“In S. cerevisiae, Hsp90 interacts physically with the catalytic subunit of calcineurin keeping it stable and poised for activation [23].”
From Hsp90 Governs Echinocandin Resistance in the Pathogenic Yeast Candida albicans via Calcineurin (2009) · cites this paper as [23]
Hsp90 and calcineurin physically interact in S. cerevisiae.
“Consistent with previous findings [23], we confirmed that Hsp90 and calcineurin physically interact in S. cerevisiae (Figure 9A), as they do in C. albicans (Figure 4).”
From Hsp90 Governs Echinocandin Resistance in the Pathogenic Yeast Candida albicans via Calcineurin (2009) · cites this paper as [23]

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Authors: Imai, J., & Yahara, I.
Affiliations: Tokyo Metropolitan Institute of Medical Science (JP)
Corresponding author: Yahara, Ichiro
ORCID: Imai, Jun
Yahara, Ichiro
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2000-12-01
Volume: 20
Issue: 24
Pages: 9262-9270
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.20.24.9262-9270.2000
PMC: PMC102183
OpenAlex: W2138281171
Cited by: 123
References: 53
Citations by year: 2025: 1 · 2024: 2 · 2023: 1 · 2022: 5 · 2021: 3 · 2020: 8 · 2019: 3 · 2018: 5 · 2017: 5 · 2016: 4 · 2015: 3 · 2014: 11 · 2013: 2 · 2012: 6
FWCI: 1.57
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
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 › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
Keywords: HSP90, calcineurin, salt tolerance, sodium chloride stress, protein stabilization, protein-protein interaction, geldanamycin, calcium/calmodulin, Saccharomyces cerevisiae
MeSH terms: Calcium-Binding Proteins, Canavanine, Cloning, Molecular, Culture Media, Heat-Shock Proteins, Phosphoprotein Phosphatases, Plasmids, Precipitin Tests, Saccharomyces cerevisiae, Salts, Temperature, Transformation, Genetic, Blotting, Western, HSP90 Heat-Shock Proteins, Calcineurin, Saccharomyces cerevisiae Proteins

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Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.

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