O2–01–07: Phosphorylation of tau at Ser214 mediates a novel interaction of tau with 14–3–3 that leads to reduction of tau aggregation | Zendy

Tanaka Toshihisa | Zendy; Sadik Golam Md. | Zendy; Nessa Begum Nurun | Zendy; Takeda Masatoshi | Zendy

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O2–01–07: Phosphorylation of tau at Ser214 mediates a novel interaction of tau with 14–3–3 that leads to reduction of tau aggregation

Author(s) -

Tanaka Toshihisa,

Sadik Golam Md.,

Nessa Begum Nurun,

Takeda Masatoshi

Publication year - 2006

Publication title -

alzheimer's and dementia

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.713

H-Index - 118

eISSN - 1552-5279

pISSN - 1552-5260

DOI - 10.1016/j.jalz.2006.05.108

Subject(s) - phosphorylation , tau protein , phosphoprotein , chemistry , kinase , serine , threonine , microbiology and biotechnology , signal transduction , protein kinase a , cyclin dependent kinase 5 , protein phosphorylation , binding site , biochemistry , biology , cyclin dependent kinase 2 , alzheimer's disease , medicine , disease , pathology

aggregated tau between cells expressing wild-type and the mutant PTEN. Moreover, we infected rat cortical primary neurons with Sindbis viruses expressing wild-type or the mutant PTEN to monitor neuronal growth. At last, we performed immunohistology to compare phospho-tau and PTEN levels between AD patient and non-AD brains. Conclusions: 1. PTEN affects tau phosphorylation at Akt and GSK-3 phosphorylation sites. 2. PTEN affects tau aggregation and binding to microtubules. 3. PTEN’s effects on tau phosphorylation are partially through PIP3/Akt signaling pathway.

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