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Harmful tau spreads like self-propagating prion proteins

Nature作者：Kayleigh Mason-Chalmers2026年9月30日正文已收录本站
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Structural studies support the idea that fibrillized tau protein, a feature of neurodegenerative disorders, acts as a prion-like template to induce misfolding in healthy tau.

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  1. Kayleigh Mason-Chalmers

    1. Kayleigh Mason-Chalmers is in the Department of Chemistry and Biochemistry, the UCLA-DOE Institute for Genomics and Proteomics, and the STROBE NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, California 90095, USA.

  2. Jose A. Rodriguez

    1. Jose A. Rodriguez is in the Department of Chemistry and Biochemistry, the UCLA-DOE Institute for Genomics and Proteomics, and the STROBE NSF Science and Technology Center, University of California, Los Angeles (UCLA), Los Angeles, California 90095, USA.

Prions are shape-shifting, self-assembling proteins that transform from a physiologically harmless version into one that is misfolded, prone to aggregation and infectious. What makes prions and prion-like proteins capable of causing disease is their ability to act as templates, forcing normal functional proteins into a toxic form. Several proteins that are associated with neurodegenerative diseases, such as amyloid-β, α-synuclein and tau, are thought to spread in a prion-like manner1,2, but experimental support for some aspects of this hypothesis and its atomic basis have been lacking. In their paper in Nature, Lövestam et al.3 show that injecting human tau fibrils into mice causes mouse tau to take on the form of the injected structures, bolstering the theory that tau propagates similarly to prions.

doi: https://doi.org/10.1038/d41586-026-02778-w

References

  1. Prusiner, S. B. Science 336, 1511–1513 (2012).

    Article  PubMed  Google Scholar 

  2. Weingarten, M. D., Lockwood, A. H., Hwo, S. Y. & Kirschner, M. W. Proc. Natl Acad. Sci. USA 72, 1858–1862 (1975).

    Article  PubMed  Google Scholar 

  3. Lövestam, S. et al. Nature https://doi.org/10.1038/s41586-026-11061-x (2026).

    Article  Google Scholar 

  4. Basheer, N. et al. Acta Neuropathol. Commun. 12, 52 (2024).

    Article  PubMed  Google Scholar 

  5. Shi, Y. et al. Nature 598, 359–363 (2021).

    Article  PubMed  Google Scholar 

  6. Fitzpatrick, A. W. P. et al. Nature 547, 185–190 (2017).

    Article  PubMed  Google Scholar 

  7. Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R. & Eisenberg, D. S. Cell 184, 4857–4873 (2021).

    Article  PubMed  Google Scholar 

  8. Wegmann, S., Medalsy, I. D., Mandelkow, E. & Müller, D. J. Proc. Natl Acad. Sci USA 110, 313–321 (2013).

    Article  Google Scholar 

  9. Scheres, S. H. W. Structure 34, 1061–1071 (2026).

    Article  PubMed  Google Scholar 

  10. Tarutani, A. et al. FEBS Open Bio 13, 1394–1404 (2023).

    Article  PubMed  Google Scholar 

  11. Duan, P. et al. J. Biol. Chem. 300, 107730 (2024).

    Article  PubMed  Google Scholar 

  12. Wang, J. et al. Structure 32, 2251–2258 (2024).

    Article  PubMed  Google Scholar 

  13. Guo, J. L. et al. J. Exp. Med. 213, 2635–2654 (2016).

    Article  PubMed  Google Scholar 

  14. Kano, M. et al. Acta Neuropathol. Commun. https://doi.org/10.1186/s40478-026-02407-7 (2026).

    Article  Google Scholar 

  15. Schweighauser, M. et al. Acta Neuropathol. Commun. 11, 160 (2023).

    Article  PubMed  Google Scholar 

  16. Rawat, P. et al. Int. J. Mol. Sci. 23, 12841 (2022).

    Article  PubMed  Google Scholar 

  17. Burger, D. et al. Nature 648, 409–417 (2025).

    Article  PubMed  Google Scholar 

  18. Hanger, D. P., Betts, J. C., Loviny, T. L., Blackstock, W. P. & Anderton, B. H. J. Neurochem. 71, 2465–2476 (1998).

    Article  PubMed  Google Scholar 

  19. Watts, J. C. & Prusiner, S. B. J. Biol. Chem. 289, 19841–19849 (2014).

    Article  PubMed  Google Scholar 

  20. Ghaemmaghami, S. et al. J. Mol. Biol. 413, 527–542 (2011).

    Article  PubMed  Google Scholar 

Download references

Competing Interests

The authors declare no competing interests.

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