Dynamics of the regulation of Hsp90 by the co‐chaperone Sti1
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In eukaryotic cells, Hsp90 chaperones assist late folding steps of many regulatory protein clients by a complex ATPase cycle. Binding of clients to Hsp90 requires prior interaction with Hsp70 and a transfer reaction that is mediated by the co-chaperone Sti1/Hop. Sti1 furthers client transfer by inhibiting Hsp90's ATPase activity. To better understand how Sti1 prepares Hsp90 for client acceptance, we characterized the interacting domains and analysed how Hsp90 and Sti1 mutually influence their conformational dynamics using hydrogen exchange mass spectrometry. Sti1 stabilizes several regions in all three domains of Hsp90 and slows down dissociation of the Hsp90 dimer. Our data suggest that Sti1 inhibits Hsp90's ATPase activity by preventing N-terminal dimerization and docking of the N-terminal domain with the middle domain. Using crosslinking and mass spectrometry we identified Sti1 segments, which are in close vicinity of the N-terminal domain of Hsp90. We found that the length of the linker between C-terminal dimerization domain and the C-terminal MEEVD motif is important for Sti1 association rates and propose a kinetic model for Sti1 binding to Hsp90.
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A 15-Å-resolution Hsp90-Hop cryo-EM structure and previous studies show that HopTPR2B can make direct contacts with Hsp90MD.
“However, the 15-Å-resolution Hsp90–Hop cryo-EM structure34 (Supplementary Fig. 7c) and previous studies33,35 show that HopTPR2B can make direct contacts with Hsp90MD.”
From Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism (2022) · cites this paper as [35]
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Self-citation
- Authors
- Lee, C., Graf, C., Mayer, F. J., Richter, S. M., & Mayer, M. P.
- Affiliations
- Heidelberg University (DE)
- Bruker (Germany) (DE)
- Corresponding author
- Mayer, Matthias P
- Venue
- The EMBO Journal
- Published
- 2012-02-21
- Volume
- 31
- Issue
- 6
- Pages
- 1518-1528
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3321184
- OpenAlex
- W2099146435
- Cited by
- 105
- References
- 35
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 10 · 2023: 2 · 2022: 6 · 2021: 7 · 2020: 7 · 2019: 6 · 2018: 5 · 2017: 9 · 2016: 11 · 2015: 5 · 2014: 14 · 2013: 11 · 2012: 5
- FWCI
- 4.50
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 638)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- HSP90, STI1, ATPase inhibition, protein-protein interaction, conformational dynamics, hydrogen-deuterium exchange mass spectrometry, crosslinking, binding kinetics, chaperone regulation
- MeSH terms
- Adenosine Triphosphatases, Binding Sites, Heat-Shock Proteins, Protein Binding, Saccharomyces cerevisiae, Protein Structure, Tertiary, Molecular Chaperones, HSP90 Heat-Shock Proteins, Dimerization, Saccharomyces cerevisiae Proteins
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