Threonine 22 Phosphorylation Attenuates Hsp90 Interaction with Cochaperones and Affects Its Chaperone Activity
Open accessAbstract
Heat shock protein 90 (Hsp90) is an essential molecular chaperone whose activity is regulated not only by cochaperones but also by distinct posttranslational modifications. We report here that casein kinase 2 phosphorylates a conserved threonine residue (T22) in α helix-1 of the yeast Hsp90 N-domain both in vitro and in vivo. This α helix participates in a hydrophobic interaction with the catalytic loop in Hsp90's middle domain, helping to stabilize the chaperone's ATPase-competent state. Phosphomimetic mutation of this residue alters Hsp90 ATPase activity and chaperone function and impacts interaction with the cochaperones Aha1 and Cdc37. Overexpression of Aha1 stimulates the ATPase activity, restores cochaperone interactions, and compensates for the functional defects of these Hsp90 mutants.
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In S. cerevisiae and C. albicans, CK2 phosphorylates Hsp90, thereby modulating chaperone function.
“In S. cerevisiae and C. albicans, CK2 phosphorylates Hsp90, thereby modulating chaperone function27,28.”
From Dual action antifungal small molecule modulates multidrug efflux and TOR signaling (2016) · cites this paper as [27]
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References 37 · Cited by 165
- Authors
- Mollapour, M., Tsutsumi, S., Truman, A. W., Xu, W., Vaughan, C. K., Beebe, K., Konstantinova, A., Vourganti, S., Panaretou, B., Piper, P. W., Trepel, J. B., Prodromou, C., Pearl, L. H., & Neckers, L.
- Affiliations
- National Cancer Institute (US)
- University of Sheffield (GB)
- Institute of Structural and Molecular Biology (GB)
- King's College London (GB)
- University of Sussex (GB)
- Corresponding author
- Neckers, Len
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-03
- Volume
- 41
- Issue
- 6
- Pages
- 672-681
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3062913
- OpenAlex
- W2002910631
- Cited by
- 165
- References
- 37
- Citations by year
- 2026: 9 · 2025: 3 · 2024: 9 · 2023: 4 · 2022: 13 · 2021: 4 · 2020: 7 · 2019: 12 · 2018: 12 · 2017: 10 · 2016: 13 · 2015: 9 · 2014: 16 · 2013: 16 · 2012: 14
- FWCI
- 7.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Sussex Research Online (University of Sussex) (submittedVersion)
- BIROn (Birkbeck, University of London) (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Kent Academic Repository (University of Kent) (submittedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- National Institutes of Health (Z99 CA999999)
- National Cancer Institute (Z01SC010074, Z01BC011032, ZIASC010074, ZIABC011032)
- 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 › Genomics and Chromatin Dynamics
- Keywords
- HSP90, casein kinase 2, co-chaperones, Aha1, Cdc37, chaperone activity, ATPase activity, post-translational modification, phosphomimetic mutations, hydrophobic interactions
- MeSH terms
- Fungal Proteins, Humans, Phosphorylation, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Threonine, Protein Structure, Secondary, Protein Structure, Tertiary, Cell Cycle Proteins, Molecular Chaperones, Chaperonins, HSP90 Heat-Shock Proteins, Saccharomyces cerevisiae Proteins, Casein Kinase II
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