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  GSK3β phosphorylation catalyzes the aggregation of tau into Alzheimer's disease-like filaments

Chakraborty, P., Ibáñez de Opakua, A., Purslow, J. A., Fromm, S. A., Chatterjee, D., Zachrdla, M., et al. (2024). GSK3β phosphorylation catalyzes the aggregation of tau into Alzheimer's disease-like filaments. Proceedings of the National Academy of Sciences of the United States of America, 121(52): e2414176121. doi:10.1073/pnas.2414176121.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0010-628E-0 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0010-628F-F
Genre: Zeitschriftenartikel
Andere : GSK3beta phosphorylation catalyzes the aggregation of tau into Alzheimer's disease-like filaments
Andere : GSK3 beta phosphorylation catalyzes the aggregation of tau into Alzheimer's disease-like filaments

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chakraborty-et-al-2024.pdf (Verlagsversion), 5MB
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https://hdl.handle.net/21.11116/0000-0010-6290-C
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 Urheber:
Chakraborty, Pijush1, Autor           
Ibáñez de Opakua, Alain, Autor
Purslow, Jeffrey A., Autor
Fromm, Simon A., Autor
Chatterjee, Debdeep, Autor
Zachrdla, Milan, Autor
Zhuang, Shannon, Autor
Puri, Sambhavi, Autor
Wolozin, Benjamin, Autor
Zweckstetter, Markus1, 2, Autor           
Affiliations:
1Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350124              
2Research Group of Protein Structure Determination using NMR, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350128              

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 Zusammenfassung: The pathological deposition of proteins is a hallmark of several devastating neurodegenerative diseases. These pathological deposits comprise aggregates of proteins that adopt distinct structures named strains. However, the molecular factors responsible for the formation of distinct aggregate strains are unknown. Here, we show that the serine/threonine kinase GSK3β catalyzes the aggregation of the protein tau into Alzheimer’s disease (AD)-like filaments. We demonstrate that phosphorylation by GSK3β, but not by several other kinases, promotes the aggregation of full-length tau as well as enhances phase separation into gel-like condensate structures. Cryoelectron microscopy further reveals that the fibrils formed by GSK3β-phosphorylated tau adopt a fold comparable to that of paired helical filaments isolated from the brains of AD patients. Our results elucidate the intricate relationship between posttranslational modification and the formation of tau strains in neurodegenerative diseases.

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Sprache(n): eng - English
 Datum: 2024-12-182024-12-24
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.2414176121
 Art des Abschluß: -

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Projektname : LLPS-NMR
Grant ID : 787679
Förderprogramm : Horizon 2020 (H2020)
Förderorganisation : European Commission (EC)

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : PNAS
  Andere : Proceedings of the National Academy of Sciences of the USA
  Kurztitel : Proc. Natl. Acad. Sci. U. S. A.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 121 (52) Artikelnummer: e2414176121 Start- / Endseite: - Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230