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Accelerated filament formation from tau protein with specific FTDP‐17 missense mutations
Author(s) -
Nacharaju Parimala,
Lewis Jada,
Easson Colin,
Yen Samuel,
Hackett Jennifer,
Hutton Mike,
Yen Shu-Hui
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00294-x
Subject(s) - missense mutation , frontotemporal dementia , neurodegeneration , parkinsonism , tau protein , tauopathy , biology , genetics , chromosome 17 (human) , dementia , mutation , neuroscience , alzheimer's disease , medicine , pathology , chromosome , disease , gene
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.