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Alzheimer's disease

Pinning down phosphorylated tau

Nature volume 399, pages 739–740 (1999)Cite this article

A defining characteristic of several neurodegenerative diseases, including Alzheimer's disease and Pick's disease, is the formation of filamentous deposits of a microtubule-associated protein called tau in an abnormally hyperphosphorylated form. The discovery of mutations in the tau gene in a condition known as ‘familial frontotemporal dementia and parkinsonism linked to chromosome 17’ has renewed interest in the mechanisms by which dysfunction of tau causes neurodegeneration.

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Figure 1: Pin1 restores the ability of phosphorylated tau to bind to microtubules.

References

  1. Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P. & Lu, K. P. Nature 399, 784–788 (1999).

    Article  ADS  CAS  Google Scholar 

  2. Lu, K. P., Hanes, S. D. & Hunter, T. Nature 380, 544–547 (1996).

    Article  ADS  CAS  Google Scholar 

  3. Yaffe, M. B. et al. Science 278, 1957–1960 (1997).

    Google Scholar 

  4. Vincent, I., Rosado, P. & Davies, P. J. Cell Biol. 132, 413–425 (1996).

    Google Scholar 

  5. Kondratick, C. M. & Vandré, D. D. J. Neurochem. 67, 2405–2416 (1996).

    Google Scholar 

  6. Pope, W. B. et al. Exp. Neurol. 126, 185–194 (1994).

    Google Scholar 

  7. Illenberger, S. et al. Mol. Biol. Cell 9, 1495–1512 (1998).

    Google Scholar 

  8. Hasegawa, M. et al. J. Biol. Chem. 267, 17047–17054 (1992).

    Google Scholar 

  9. Watanabe, A. et al. J. Biol. Chem. 268, 25712–25717 (1993).

    Google Scholar 

  10. Ishiguro, K. et al. FEBS Lett. 325, 167–172 (1993).

    Google Scholar 

  11. Goedert, M. et al. Biochem. J. 301, 871–877 (1994).

    Google Scholar 

  12. Matsuo, E. S. et al. Neuron 13, 989–1002 (1994).

    Google Scholar 

  13. Morishima-Kawashima, M. et al. J. Biol. Chem. 270, 823–829 (1995).

    Google Scholar 

  14. Goedert, M., Crowther, R. A. & Spillantini, M. G. Neuron 21, 955–958 (1998).

    Google Scholar 

  15. Vincent, I., Jicha, G., Rosado, M. & Dickson, D. W. J. Neurosci. 17, 3588–3598 (1997).

    Google Scholar 

  16. Nagy, Zs., Esiri, M. M., Cato, A.-M. & Smith, A. D. Acta Neuropathol. 94, 6–15 (1997).

    Google Scholar 

  17. Busser, J., Geldmacher, D. S. & Herrup, K. J. Neurosci. 18, 2801–2807 (1998).

    Google Scholar 

Download references

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  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Michel Goedert

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  1. Michel Goedert
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Goedert, M. Pinning down phosphorylated tau. Nature 399, 739–740 (1999). https://doi.org/10.1038/21550

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