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P70 S6 kinase mediates tau phosphorylation and synthesis
Author(s) -
Pei Jin-Jing,
An Wen-Lin,
Zhou Xin-Wen,
Nishimura Takeshi,
Norberg Jan,
Benedikz Eirikur,
Götz Jürgen,
Winblad Bengt
Publication year - 2006
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/j.febslet.2005.11.059
Subject(s) - p70 s6 kinase 1 , phosphorylation , immunoprecipitation , tau protein , chemistry , kinase , microbiology and biotechnology , translation (biology) , downregulation and upregulation , biology , alzheimer's disease , medicine , protein kinase b , biochemistry , messenger rna , disease , gene
Currently, we found that the 70‐kDa p70 S6 kinase (p70S6K) directly phosphorylates tau at S262, S214, and T212 sites in vitro. By immunoprecipitation, p‐p70S6K (T421/S424) showed a close association with p‐tau (S262 and S396/404). Zinc‐induced p70S6K activation could only upregulate translation of total S6 and tau but not global proteins in SH‐SY5Y cells. The requirement of p70S6K activation was confirmed in the SH‐SY5Y cells that overexpress wild‐type htau40. Level of p‐p70S6K (T421/S424) was only significantly correlated with p‐tau at S262, S214, and T212, but not T212/S214, in Alzheimer's disease (AD) brains. These suggested that p70S6K might contribute to tau related pathologies in AD brains.