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Regulation of α-synuclein by chaperones in mammalian cells
Open accessAbstract
Neurodegeneration in patients with Parkinson's disease is correlated with the occurrence of Lewy bodies-intracellular inclusions that contain aggregates of the intrinsically disordered protein α-synuclein 1. The aggregation propensity of α-synuclein in cells is modulated by specific factors that include post-translational modifications 2,3, Abelson-kinase-mediated phosphorylation 4,5 and interactions with intracellular machineries such as molecular chaperones, although the underlying mechanisms are unclear 6-8. Here we systematically characterize the interaction of molecular chaperones with α-synuclein in vitro as well as in cells at the atomic level. We find that six highly divergent molecular chaperones commonly recognize a canonical motif in α-synuclein, consisting of the N terminus and a segment around Tyr39, and hinder the aggregation of α-synuclein. NMR experiments 9 in cells show that the same transient interaction pattern is preserved inside living mammalian cells. Specific inhibition of the interactions between α-synuclein and the chaperone HSC70 and members of the HSP90 family, including HSP90β, results in transient membrane binding and triggers a remarkable re-localization of α-synuclein to the mitochondria and concomitant formation of aggregates. Phosphorylation of α-synuclein at Tyr39 directly impairs the interaction of α-synuclein with chaperones, thus providing a functional explanation for the role of Abelson kinase in Parkinson's disease. Our results establish a master regulatory mechanism of α-synuclein function and aggregation in mammalian cells, extending the functional repertoire of molecular chaperones and highlighting new perspectives for therapeutic interventions for Parkinson's disease.
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“This suggests that Hsp90 has a holdase function for these proteins by binding and protecting them from aggregation (69).”
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Gerez, J., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Fleischmann, Y., Güntert, P., & Riek, R. (2022) · Communications Biology · doi:10.1038/s42003-022-04251-6 · Cited by 23
Self-citationBeriashvili, D., Yao, R., D’Amico, F., Krafčíková, M., Gurinov, A., Safeer, A., Cai, X., Mulder, M. P. C., Liu, Y., Folkers, G. E., et al. (2023) · Chemical Science · doi:10.1039/d3sc02117c · Cited by 24
Structural basis of DegP protease temperature-dependent activation
Šulskis, D., Thoma, J., & Burmann, B. M. (2021) · Science Advances · doi:10.1126/sciadv.abj1816 · Cited by 23
Self-citationMultivalent protein–protein interactions are pivotal regulators of eukaryotic Hsp70 complexes
Johnson, O. T., & Gestwicki, J. E. (2022) · Cell Stress and Chaperones · doi:10.1007/s12192-022-01281-1 · Cited by 23
Fatal attraction – The role of hypoxia when alpha-synuclein gets intimate with mitochondria
Burtscher, J., Syed, M. M. K., Keller, M. A., Lashuel, H. A., & Millet, G. P. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.07.017 · Cited by 25
Biomolecular Perturbations in In-Cell Dynamic Nuclear Polarization Experiments
Overall, S. A., & Barnes, A. B. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.743829 · Cited by 22
Xiao, Y., Ghosh, R., & Frederick, K. K. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.789478 · Cited by 21
Chopra, G., Shabir, S., Yousuf, S., Kauts, S., Bhat, S. A., Mir, A. H., & Singh, M. P. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03042-8 · Cited by 24
Schorova, L., Bedard, N., Khayachi, A., Ho, H.-H., Bolivar-Pedroso, J., Huynh, J., Piccirelli, M., Wang, Y., Plourde, M., Luo, W., et al. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00601-1 · Cited by 20
Abdelaziz, A. M. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114692 · Cited by 20
A RaPID Macrocyclic Peptide That Inhibits the Formation of α‐Synuclein Amyloid Fibrils
Ikenoue, T., Oono, M., So, M., Yamakado, H., Arata, T., Takahashi, R., Kawata, Y., & Suga, H. (2023) · ChemBioChem · doi:10.1002/cbic.202300320 · Cited by 21
Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein
Ohgita, T., Kono, H., Morita, I., Oyama, H., Shimanouchi, T., Kobayashi, N., & Saito, H. (2023) · Scientific Reports · doi:10.1038/s41598-023-38070-4 · Cited by 20
Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy
Karamanos, T. K., & Clore, G. M. (2022) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-090921-120150 · Cited by 20
The inhibitory action of the chaperone BRICHOS against the α-Synuclein secondary nucleation pathway
Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P., Krainer, G., Andrzejewska, E. A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54212-2 · Cited by 19
Self-citationPons, M., Loftus, N. J., Vialaret, J., Moreau, S., Lehmann, S., & Hirtz, C. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.818606 · Cited by 20
UBA52 Attunes VDAC1-Mediated Mitochondrial Dysfunction and Dopaminergic Neuronal Death
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Cellular Applications of DNP Solid‐State NMR – State of the Art and a Look to the Future
Beriashvili, D., Zhou, J., Liu, Y., Folkers, G. E., & Baldus, M. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202400323 · Cited by 19
Metadata
- Authors
- Burmann, B. M., Gerez, J. A., Matečko-Burmann, I., Campioni, S., Kumari, P., Ghosh, D., Mazur, A., Aspholm, E. E., Šulskis, D., Wawrzyniuk, M., Bock, T., Schmidt, A., Rüdiger, S. G. D., Riek, R., & Hiller, S.
- Affiliations
- University of Basel (CH)
- ETH Zurich (CH)
- Wallenberg Centre for Molecular and Translational Medicine (SE)
- Utrecht University (NL)
- Corresponding author
- Burmann, Björn M.
- Riek, Roland
- Hiller, Sebastian
- ORCID
- Venue
- Nature
- Published
- 2019-12-04
- Volume
- 577
- Issue
- 7788
- Pages
- 127-132
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC6930850
- OpenAlex
- W2992154881
- Cited by
- 255
- References
- 38
- Citations by year
- 2026: 12 · 2025: 32 · 2024: 38 · 2023: 56 · 2022: 53 · 2021: 36 · 2020: 27 · 2019: 1
- FWCI
- 20.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- edoc (University of Basel) (acceptedVersion, other-oa)
- PubMed Central (acceptedVersion)
- edoc (University of Basel) (acceptedVersion)
- DORA Empa (Swiss Federal Laboratories for Materials Science and Technology (Empa)) (submittedVersion, other-oa)
- RePEc: Research Papers in Economics (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Gothenburg University Publications Electronic Archive (Gothenburg University) (submittedVersion)
- edoc (University of Basel)
- Funders
- National Science Foundation
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (166426, 148238, 164425, 128419)
- Vetenskapsrådet
- Göteborgs Universitet
- Wallenberg Centre for Molecular and Translational Medicine
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- alpha-synuclein, molecular chaperones, Parkinson's disease, protein aggregation, Hsc70, HSP90, HSP90β, Abelson kinase, mitochondrial localization, Lewy bodies, intrinsically disordered proteins, neurodegeneration
- MeSH terms
- Cell Survival, Humans, Magnetic Resonance Spectroscopy, Protein Processing, Post-Translational, Molecular Chaperones, alpha-Synuclein, HEK293 Cells
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