“…On the other hand, mTORC2, but not mTORC1, can phosphorylate AKT, and this phosphorylation which leads to optimal activation of AKT, is not acutely sensitive to rapamycin [64,130]. Although AKT phosphorylation at its conserved hydrophobic motif site is used as a hallmark of mTORC2 activity, other direct substrates of mTORC2, such as SGK and PKC, are emerging from recent studies [164]. mTORC2 has also been linked to other cellular functions, such as actin cytoskeleton reorganization, translation, and protein maturation/folding [111].…”