From http://en.wikipedia.org/wiki/P70S6_kinase...

Phosphorylation of S6 induces protein synthesis at the ribosome.

P70S6 kinase is in a signaling pathway that includes mTOR (the mammalian target of rapamycin). mTOR can be activated in distinct ways, thereby activating p70S6K. For example, branched chain amino acids such as leucine are sufficient to activate mTOR, resulting in an increase in p70S6K phosphorylation (and thereby activating it). mTOR is also in a pathway downstream of the kinase Akt. Akt is typically activated upon stimulation of a cell with a growth factor (such as IGF-1). Akt then activates mTOR (by inhibiting the Tsc complex), leading to p70S6K activation.

We also found a paper showing that downregulation of S6 kinase also results in a decrease in protein translation in yeast (but I'm waiting for Matt Kaeberlein to email me the slides from yesterday).

  • 2
    $\begingroup$ Could you please summarize the potential link between S6kinase and neurons? Your question seems to rely entirely on an abstract and lacks context. $\endgroup$
    – Abe
    Commented Mar 11, 2012 at 6:43
  • $\begingroup$ S6 kinase is involved in protein translation. Long-term potentiation relies on protein creation. So fewer proteins are made with reduced S6 kinase levels, which could imply slower rates of memory formation through LTP $\endgroup$ Commented Mar 11, 2012 at 19:14

1 Answer 1


I can't rule it out, but it sounds a lot like trying to tune a piano with sledgehammer.

Neuronal LTP depends on protein translation, but so does absolutely everything else in the cell. Inhibiting protein synthesis at the ribosome will block the formation of all proteins, not just the ones responsible for LTP. Unless there's a link I don't know about between LTP and total levels of protein translation, you're really going to want to look into inhibiting the production of proteins specifically responsible for LTP and not protein synthesis in general.


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