Accelerated filament formation from tau protein with specific FTDP-17 missense mutations

Parimala Nacharaju, Jada Lewis, Colin Easson, Samuel Yen, Jennifer Hackett, Mike Hutton, Shu Hui Yen

Research output: Contribution to journalArticlepeer-review

226 Scopus citations

Abstract

Tau is the major component of the neurofibrillar tangles that are a pathological hallmark of Alzheimers' disease. The identification of missense and splicing mutations in tau associated with the inherited frontotemporal dementia and Parkinsonism linked to chromosome 17 demonstrated that tau dysfunction can cause neurodegeneration. However, the mechanism by which tau dysfunction leads to neurodegeneration remains uncertain. Here, we present evidence that frontotemporal dementia and Parkinsonism linked to chromosome 17 missense mutations, P301L, V337M and R406W, cause an accelerated aggregation of tau into filaments. These results suggest one mechanism by which these mutations can cause neurodegeneration and frontotemporal dementia and Parkinsonism linked to chromosome 17. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)195-199
Number of pages5
JournalFEBS Letters
Volume447
Issue number2-3
DOIs
StatePublished - Mar 26 1999

Keywords

  • Frontotemporal dementia and Parkinsonism linked to chromosome 17
  • Neurodegeneration
  • Tau mutation
  • Tau polymerization
  • Tauopathy

ASJC Scopus subject areas

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

Fingerprint Dive into the research topics of 'Accelerated filament formation from tau protein with specific FTDP-17 missense mutations'. Together they form a unique fingerprint.

Cite this