A signal transduction pathway leading to the phosphorylation and activation of mTOR in response to insulin

A signal transduction pathway leading to the phosphorylation and activation of mTOR in response to insulin. Binding of insulin to its receptor activates the receptor tyrosine kinase, which phosphorylates insulin receptor substrate (IRS)-1 and/or –2 (). Phosphotyrosyl residues in these proteins serve as docking sites for PI 3-kinase, whose activation leads to activation of PKB. As described in the text, activation of PKB results in phosphorylation and activation of mTOR, although we stress that other kinases may be involved. Once activated, mTOR phosphorylates the translational repressor, PHAS-I, which dissociates from eIF-4E, thereby increasing the amount of eIF-4E available to mediate translation initiation ().

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Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway. (1998) Pamela H. Scott, et al. Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7772-7777. Figure: F6. All organisms Mus musculus Homo sapiens Drosophila melanogaster

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