Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation

R. Dayanandan, M. Van Slegtenhorst, T. G.A. Mack, L. Ko, S. H. Yen, K. Leroy, J. P. Brion, B. H. Anderton, M. Hutton, S. Lovestone

Research output: Contribution to journalArticlepeer-review

169 Scopus citations

Abstract

In vitro evidence has suggested a change in the ability of tau bearing mutations associated with fronto-temporal dementia to promote microtubule assembly. We have used a cellular assay to quantitate the effect of both isoform differences and mutations on the physiological function of tau. Whilst all variants of tau bind to microtubules, microtubule extension is reduced in cells transfected with 3-relative to 4-repeat tau. Mutations reduce microtubule extension with the P301L mutation having a greater effect than the V337M mutation. The R406W mutation had a small effect on microtubule extension but, surprisingly, tau with this mutation was less phosphorylated in intact cells than the other variants. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)228-232
Number of pages5
JournalFEBS Letters
Volume446
Issue number2-3
DOIs
StatePublished - Mar 12 1999

Keywords

  • Fronto-temporal degeneration
  • GSK-3
  • Microtubule
  • Mutation
  • Tau

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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