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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.