P70 S6 Kinase Mediates Tau Phosphorylation and Synthesis

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2005 Dec 21

PMID 16364302

Citations 55

Authors

Jin-Jing Pei

Wen-Lin An

Xin-Wen Zhou

Takeshi Nishimura

Jan Norberg

Eirikur Benedikz

Jurgen Gotz

Bengt Winblad

Affiliations

Soon will be listed here.

Abstract

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.

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