Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation
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Hsp90 is an essential molecular chaperone in the eukaryotic cytosol. Its function is modulated by cochaperones and posttranslational modifications. Importantly, the phosphatase Ppt1 is a dedicated regulator of the Hsp90 chaperone system. Little is known about Ppt1-dependent phosphorylation sites and how these affect Hsp90 activity. Here, we identified the major phosphorylation sites of yeast Hsp90 in its middle or the C-terminal domain and determined the subset regulated by Ppt1. In general, phosphorylation decelerates the Hsp90 machinery, reduces chaperone function in vivo, sensitizes yeast cells to Hsp90 inhibition and affects DNA repair processes. Modification of one particular site (S485) is lethal, whereas others modulate Hsp90 activity via distinct mechanisms affecting the ATPase activity, cochaperone binding and manipulating conformational transitions in Hsp90. Our mechanistic analysis reveals that phosphorylation of Hsp90 permits a regulation of the conformational cycle at distinct steps by targeting switch points for the communication of remote regions within Hsp90.
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Multiple phosphorylation sites have been identified as regulatory elements of Hsp90 function in human and yeast.
“Multiple phosphorylation sites have been identified as regulatory elements of Hsp90 function in human and yeast (13–15).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [15]
Four serine residues (S379, S485, S602, and S604) in S. cerevisiae Hsp90 play some role in Hsp90 function.
“Four serine residues were found to play some role in Hsp90 function (S379, S485, S602, and S604).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [15]
A similar mass spectrometric analysis in S. cerevisiae identified 10 phosphorylation sites in Hsp90.
“A similar mass spectrometric analysis in the yeast S. cerevisiae identified 10 phosphorylation sites in Hsp90 (15).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [15]
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- Authors
- Soroka, J., Wandinger, S. K., Mäusbacher, N., Schreiber, T., Richter, K., Daub, H., & Buchner, J.
- Affiliations
- Center for Integrated Protein Science Munich (DE)
- Max Planck Society (DE)
- Max Planck Institute of Biochemistry (DE)
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 45
- Issue
- 4
- Pages
- 517-528
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1985532753
- Cited by
- 139
- References
- 69
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 11 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 16 · 2019: 11 · 2018: 15 · 2017: 12 · 2016: 5 · 2015: 9 · 2014: 14 · 2013: 11 · 2012: 5
- FWCI
- 5.01
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 532 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Funders
- Verband der Chemischen Industrie
- Deutsche Forschungsgemeinschaft
- 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 › Protein Structure and Dynamics
- Keywords
- HSP90, phosphorylation sites, conformational switching, molecular chaperones, ATPase activity, DNA repair, yeast, post-translational modification
- MeSH terms
- Fungal Proteins, Models, Molecular, Phosphorylation, Mass Spectrometry, Yeasts, Protein Structure, Tertiary, HSP90 Heat-Shock Proteins
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