P70 S6 kinase mediates tau phosphorylation and synthesis.

Jin-Jing Pei, Wen-Lin An, Xin-Wen Zhou, Takeshi Nishimura, Jan Norberg, Eirikur Benedikz, Jürgen Götz, Bengt Winblad

Journal: FEBS letters 2006;580(1):107-14

PMID: 16364302

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.

Address: Department of Neurotec, Division of Experimental Geriatrics, Karolinska Institutet, KFC Novum, Plan 4, SE-141 86, Huddinge, Sweden. [email protected]

DOI: 10.1016/j.febslet.2005.11.059

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MeSH Terms: Alzheimer Disease, Cell Line, Tumor, Cell-Free System, Enzyme Activation, Humans, Membrane Proteins, Phosphorylation, Protein Biosynthesis, Ribosomal Protein S6 Kinases, 70-kDa, Serine, Threonine, Zinc