"Phosphorylation of TSC2 by Akt1 inhibits its GTPase activity leading to increased GTP loading on Rheb and consequent increase in mTORC1 activity."
"Activated AKT1 modulates MTORC1 signaling in different ways : On the one hand, several studies indicate that AKT1 is able to phosphorylate TSC2 and thereby activate the TSC1/2 complex [XREF_BIBR]."
"Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo."
"TORC1 is activated by an Akt1-dependent derepression mechanism: Through phosphorylation of the (TORC1) negative regulator Tsc2 by Akt1, the GTPase Ras homolog enriched in brain (Rheb) and consequently TORC1 are activated. xref TORC1 activity is central to the control of growth and metabolism, acting as a nutrient sensor for growth regulation. xref Hence, Akt1 serves as a link between InR and TOR pathways."
"Phosphorylation of TSC2 by Akt1 inhibits its GTPase activity leading to increased GTP loading on Rheb and consequent increase in mTORC1 activity (see reviews xref – xref and references therein)."
"Active AMPK positively regulates the activity of the TSC1 and TSC2 complex by phosphorylating the TSC2 protein (resulting in the opposite activity to the AKT-1 phosphorylation of TSC2), which then turns off the RHEB G protein and reduces TOR activity [XREF_BIBR]."
"Upon insulin stimulation, PI3K activates protein kinase B (Akt and PKB), which then directly phosphorylates TSC2 resulting in the dissociation of the TSC1/2 complex from lysosomes where mTORC1 activation takes place 2."
"This is accomplished by AKT-1 phosphorylation and inactivation of TSC2 [ xref - xref ], which forms a TSC1–TSC2 protein complex that is a GAP for the RHEB G-protein."