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

Research output: Contribution to journalJournal articleResearchpeer-review


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.

Original languageEnglish
JournalF E B S Letters
Issue number1
Pages (from-to)107-14
Number of pages8
Publication statusPublished - 9 Jan 2006
Externally publishedYes


  • Alzheimer Disease
  • Cell Line, Tumor
  • Cell-Free System
  • Enzyme Activation
  • Humans
  • Journal Article
  • Membrane Proteins
  • Phosphorylation
  • Protein Biosynthesis
  • Research Support, Non-U.S. Gov't
  • Ribosomal Protein S6 Kinases, 70-kDa
  • Serine
  • Threonine
  • Zinc

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