Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle

Reidy, Michael; Kumar, Shailesh; Anderson, D Eric; Masison, Daniel C

doi:10.1534/genetics.118.301178

Cited by 22Heat shock proteins researchUbiquitin and proteasome pathwaysFungal and yeast genetics research

Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle

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Reidy, Michael, Kumar, Shailesh, Anderson, D Eric, Masison, Daniel C·2018·Genetics

DOI 10.1534/genetics.118.301178PMC PMC6063237

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Abstract

Hsp70/Hsp90 co-chaperone Sti1/Hop bridges Hsp70 and Hsp90 to facilitate client transfer. Many Hsp90 mutations make Sti1 necessary for viability, implying the Hsp90-Hsp70 interaction is essential. These mutations cluster in regions important for... The Hsp90 chaperone is regulated by many cochaperones that tune its activities, but how they act to coordinate various steps in the reaction cycle is unclear. The primary role of Saccharomyces cerevisiae Hsp70/Hsp90 cochaperone Sti1 (Hop in mammals) is to bridge Hsp70 and Hsp90 to facilitate client transfer. Sti1 is not essential, so Hsp90 can interact with Hsp70 in vivo without Sti1. Nevertheless, many Hsp90 mutations make Sti1 necessary. We noted that Sti1-dependent mutations cluster in regions proximal to N-terminal domains (SdN) or C-terminal domains (SdC), which are known to be important for interaction with Hsp70 or clients, respectively. To uncover mechanistic details of Sti1–Hsp90 cooperation, we identified intramolecular suppressors of the Hsp90 mutants and assessed their physical, functional, and genetic interactions with Hsp70, Sti1, and other cochaperones. Our findings suggest Hsp90 SdN and SdC mutants depend on the same interaction with Sti1, but for different reasons. Sti1 promoted an essential Hsp70 interaction in the SdN region and supported SdC-region function by establishing an Hsp90 conformation crucial for capturing clients and progressing through the reaction cycle. We find the Hsp70 interaction and relationship with Sti1/Hop is conserved in the human Hsp90 system. Our work consolidates and clarifies much structural, biochemical, and computational data to define in vivo roles of Sti1/Hop in coordinating Hsp70 binding and client transfer with progression of the Hsp90 reaction cycle.

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Hsp90 mutations (yHsp82 W585T and M593T, corresponding to hHsp90α W606 and M614) that would destabilize the HopDP2-Hsp90A interface cause yeast growth defects.
“Supporting our observations, Hsp90 mutations (yHsp82 W585T and M593T, corresponding to hHsp90α W606 and M614) that would destabilize the HopDP2–Hsp90A interface (Fig. 2d) cause yeast growth defects36.”
From Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism (2022) · cites this paper as [36]

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Sti1/Hop Plays a Pivotal Role in Hsp90 Regulation Beyond Bridging Hsp70
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Self-citation

Authors: Reidy, M., Kumar, S., Anderson, D. E., & Masison, D. C.
Affiliations: National Institutes of Health (US)
Corresponding author: Masison, Daniel C
ORCID: Reidy, Michael
Anderson, D Eric
Masison, Daniel C
Venue: Genetics
Publisher: Oxford University Press (OUP)
Published: 2018-06-21
Volume: 209
Issue: 4
Pages: 1139-1154
ISSN: 0016-6731 (ISSN-L)
1943-2631
DOI: 10.1534/genetics.118.301178
PMC: PMC6063237
OpenAlex: W2809647727
Cited by: 22
References: 61
Citations by year: 2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 6 · 2020: 4 · 2019: 3 · 2018: 1
FWCI: 1.24
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
Locations: Genetics (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Diabetes and Digestive and Kidney Diseases
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords: HSP90, HSP70, co-chaperones, Saccharomyces cerevisiae
MeSH terms: Binding Sites, Heat-Shock Proteins, Models, Molecular, Mutation, Protein Binding, Protein Conformation, Saccharomyces cerevisiae, Gene Expression Regulation, Fungal, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Protein Transport, trans-Golgi Network, Saccharomyces cerevisiae Proteins, Septins

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Dual Roles for Yeast Sti1/Hop in Regulating the Hsp90 Chaperone Cycle

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