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

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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

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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  1. 10.1128/mcb.9.9.3919-3930.1989 · DOI · Paper page
  2. Klee, C. B., Draetta, G. F., and Hubbard, M. J.. 1988. Calcineurin. Adv. Enzymol. Relat. Areas Mol. Biol. 61:149–200

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Metadata

Authors
Imai, J., & Yahara, I.
Affiliations
Tokyo Metropolitan Institute of Medical Science (JP)
Corresponding author
Yahara, Ichiro
Venue
Molecular and Cellular Biology
Published
2000-12-01
Volume
20
Issue
24
Pages
9262-9270
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
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
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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