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- W2042171021 abstract "Neurofibrillary tangle-bearing neurons, a pathological hallmark of Alzheimer's disease, are mostly devoid of normal microtubule (MT) structure and instead have paired helical filaments that are composed of abnormal hyperphosphorylated tau. However, a causal relationship between tau phosphorylation and MT disruption has not been clarified. To examine whether MT disruption induces tau phosphorylation, stathmin, an MT-disrupting protein, was co-expressed with tau in COS-7 cells. Stathmin expression induced apparent MT catastrophe and tau hyperphosphorylation at Thr-181, Ser-202, Thr-205, and Thr-231 sites. In contrast, c-Jun N-terminal kinase activation, or phosphatase inhibition, led to significant tau phosphorylation without affecting MT structure. These findings suggest that MT disruption induces subsequent tau phosphorylation." @default.
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- W2042171021 date "2010-06-16" @default.
- W2042171021 modified "2023-10-01" @default.
- W2042171021 title "Microtubule destruction induces tau liberation and its subsequent phosphorylation" @default.
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- W2042171021 doi "https://doi.org/10.1016/j.febslet.2010.06.014" @default.
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