"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"
No evidence text available
"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."
"The rictor-mtor complex directly phosphorylated akt/pkb on ser473 in vitro and facilitated thr308 phosphorylation by pdk1"
"Furthermore, purified PDK-1 and immuno-precipitated mTOR readily phosphorylated purified Akt1 at T308 and S473 in vitro , respectively, regardless of whether or not TCN-P was present in the reaction mixture ( xref )."
"Akt-1 is also phosphorylated at S473 by the mammalian target of Rapamycin (mTOR) complex referred to as (Rapamycin-insensitive companion of mTOR and mLST8 complex) mTORC2 [XREF_BIBR - XREF_BIBR]."
"Of note, the S473D mutant of Akt1 and Akt1 phosphorylated in Ser 473 by the rictor-mTOR complex are better targets of PDK1 than nonphosphorylated Akt1 xref ."