IndraLab

"Recent studies demonstrate that the mTOR downstream target S6K1 directly phosphorylates IRS1 serine residues, including Ser 302/307, Ser 307/312, Ser 632/636, and Ser 1097/1101."

"Furthermore, a short-term osmotic stress induces the phosphorylation of IRS1 on serine 307 by an mTOR dependent pathway (Gual et al."

"Acute osmotic stress (from 10 to 30 min of sorbitol cell treatment) induces the phosphorylation of IRS1 on Ser 307 by a mTOR dependent pathway (Gual et al."

"MTOR being a central regulator of amino acid and insulin signaling, under amino acid abundance, it phosphorylates IRS1 (at serine 307) and inhibits the downstream insulin signaling."

"The findings of the present study of diet-and obesity induced insulin resistance in murine models suggest that suppression of TSC1 by IKKbeta activates mTOR and S6K1, which in turn phosphorylate IRS1 at Ser636/639 and Ser307, thereby inhibiting IRS1 function)."

"Activation of the mTOR pathway functions as a feedback regulator of insulin action by increasing phosphorylation of IRS1 at Ser307 [pIRS (S307)] and Ser636/639 [pIRS (S636/639)] by S6K1 and mTOR, respectively."

"These results indicate that activation of protein kinase c stimulates a kinase which can phosphorylate insulin receptor substrate-1 at serine 612, resulting in an inhibition of insulin signaling in the cell these data suggest that: 1) activation of pkctheta contributes to ikk and jnk activation by ffas;2) ikk and jnk mediate pkctheta signals for irs-1 serine phosphorylation and degradation; ser-302 phosphorylation is dependent on pi 3-kinase/mtor, whereas ser-307 depends on c-jun nh2-terminal kinase to inhibit irs1 tyrosine phosphorylation. Ser-636 is located around the pi 3-kinase binding site and, therefore, thought to inhibit pi 3-kinase signaling."

"MTOR and its downstream effector S6K1 suppress IRS1 activity by directly phosphorylating IRS1 at Ser636 and Ser639 and Ser307, respectively, which leads to desensitization of insulin signaling."

"Recent studies demonstrate that the mTOR downstream target S6K1 directly phosphorylates IRS1 serine residues, including Ser 302/307, Ser 307/312, Ser 632/636, and Ser 1097/1101."

"Mtor induced the serine phosphorylation of irs-1 (ser-636/639), and such phosphorylation was inhibited by rapamycin. These results suggest that tnf impairs insulin signaling through irs-1 by activation of a pi 3-kinase/akt/mtor pathway, which is antagonized by pten"

"Although the direct phosphorylation sites targeted by mTOR and p70S6 kinase are disputed XREF_BIBR, inhibition of mTOR by rapamycin significantly reduces phosphorylation of IRS-1 residues S302, S307 and S318 XREF_BIBR."

"This result prompted us to examine whether IKKβ-derived phosphorylation of TSC1 can serve as a switch for TNFα- and mTOR-induced phosphorylation of IRS1 at Ser307 and Ser636/639."

"As part of negative feedback loop S6K activation downstream of mTOR phosphorylates IRS-1 at S307 stimulating the interaction of IRS-1 with the substrate recognition subunit FBW8 and recruiting the SCF[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"Furthermore, the mammalian target of rapamycin (mTOR) inhibitor rapamycin prevented the osmotic shock induced phosphorylation of IRS-1 on Ser307."

"Short-term osmotic stress induces the phosphorylation of IRS-1 on Ser307 by an mTOR dependent pathway."

"Although the direct phosphorylation sites targeted by mTOR and p70S6 kinase are disputed XREF_BIBR, inhibition of mTOR by rapamycin significantly reduces phosphorylation of IRS-1 residues S302, S307 and S318 XREF_BIBR."