IndraLab
Statements
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"Two phosphorylation events are necessary for maximal activation of Akt, namely phosphorylation at Thr308 and Ser473 in Akt1 (Thr309/Ser474 in Akt2 and Thr305/Ser472 in Akt3) by phosphoinositide-dependent protein kinase 1 (PDK1) and the mechanistic target of rapamycin (mTOR) complex 2 (mTORC2), respectively [ xref , xref ]."
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"The Ser 473 phosphorylation of Akt1 by the mechanistic target of rapamycin complex 2 (mTORC2) is controlled by PI3 kinase activation in cells treated with growth factors [ xref , xref ]; however, studies have yet to elucidate the mechanism by which m TORC2 kinase is recruited to the signaling complex containing Akt."
"Mammalian TOR complex 1 (mTORC1) and mTORC2 exert their actions by regulating other important kinases, such as S6 kinase (S6K) and Akt.Recent findings have revealed novel important roles for mTORC2 in the phosphorylation of AGC kinase family members. mTORC2 phosphorylates and activates Akt, SGK, and PKC, which regulate cell survival, cell cycle progression and anabolism"
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"Insulin binds to the insulin receptor (INS-R) to initiate the insulin pathway signaling cascade via insulin receptor substrate (IRS) and phosphatidylinositol-3-kinase and serine/threonine protein kinase B (PKB/AKT), which is phosphorylated at serine 473 by the mechanistic target of rapamycin complex (mTORC) 2 (mTORC2), and activates an array of downstream targets including mTORC1 to initiate protein synthesis (5–11)."
"Protein kinase B (PKB, Akt) is a Ser/Thr kinase involved in the regulation of cell survival, proliferation, and metabolism and is activated by dual phosphorylation on Thr(308) in the activation loop and Ser(473) in the hydrophobic motif. It plays a contributory role to platelet function, although little is known about its regulation. In this study, we investigated the role of the mammalian target of rapamycin complex (mTORC)-2 in Akt regulation using the recently identified small molecule ATP competitive mTOR inhibitors PP242 and Torin1."