Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1.

By D. Guertin, Deanna M Stevens, C. Thoreen, A. Burds, Nada Y. Kalaany, Jason Moffat, Michael Brown, Kevin Fitzgerald, David M. Sabatini. Developmental Cell, 2006

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Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/27c0e0884a2c28e65d368245ad0b99cae77409c0

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FoxO3 controls autophagy in skeletal muscle in vivo. (2007, background): “Furthermore , rapamycin was not able to reverse the inhibitory effect of activated Akt in preventing the upregulation of autophagy-related genes induced by fasting. mTOR is part of two multiprotein complexes: mTORC1, which contains raptor and is rapamycin sensitive, is required for signaling to S6K ”
Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “Akt is also phosphorylated at Ser473, which has been shown to regulate the specificity of Akt toward its substrates, and/or to stabilize its active conformation (Guertin et al. 2006; Ikenoue et al. 2008).”
mTOR signaling in growth control and disease (2012, background): “In addition to its role on regulating cell survival downstream of Akt and SGK1, mTORC2 has also been shown to positively control vascular system formation (Guertin et al., 2006) and chemotaxism (Liu et al.”
Defining the role of mTOR in cancer. (2007, background): “Moreover, ablation of S473 phosphorylation that occurs upon deleting rictor, mlst8, or msin1 does not eliminate T308 phosphorylation (Guertin et al., 2006b; Jacinto et al., 2006; Shiota et al., 2006).”
SREBP Activity Is Regulated by mTORC1 and Contributes to Akt-Dependent Cell Growth (2008, background): “An involvement of raptor in the regulation of lipogenesis is also consistent with its essential function during mouse development (Guertin et al., 2006).”
Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models (2011, background): “TORC2 is required for Akt phosphorylation and activation [6].”
Immunoregulatory Functions of mTOR Inhibition (2009, background): “Subsequent work has identified mTOR as an atypical serine/threonine protein kinase with a central role in mammalian developmen”
Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress (2010, background): “In contrast to the situation with mTORC1, mLST8 is required for mTORC2 function in vivo and its kinase activity in vitro (Guertin et al., 2006).”
Proliferation, survival and metabolism: the role of PI3K/AKT/mTOR signalling in pluripotency and cell fate determination (2016, background): “5; severe vasculature defects (Guertin et al., 2006) Rictor−/− Embryonic lethal at E10.”
Regulation of Immune Responses by mTOR (2011, background): “However, several studies have clearly demonstrated that Akt’s ability to regulate Forkhead box protein O1 (FOXO1) and FOXO3 is mTORC2 dependent (42).”
Identification and characterization of NVP-BEZ235, a new orally available dual phosphatidylinositol 3-kinase/mammalian target of rapamycin inhibitor with potent in vivo antitumor activity (2008, background): “Several pieces of evidence suggest that the PDK2 activity is primarily due to the mTORC2 complex and that this enzyme has no influence on the phosphorylation of Thr308 (4, 46).”
Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling (2008, background): “Deletion of mTORC2-specific subunits, such as Rictor or Sin1, abolishes the HM phosphorylation of Akt but not S6K, indicating the high substrate specificity of the two TOR complexes (Guertin et al, 2006; Jacinto et al, 2006; Shiota et al, 2006; Yang et al, 2006).”
Active-Site Inhibitors of mTOR Target Rapamycin-Resistant Outputs of mTORC1 and mTORC2 (2009, background): “Previous analysis of mTORC2 function using RNAi revealed a role for mTORC2 in the control of the actin cytoskeleton [3,4], yet these findings were not confirmed in primary MEFs lacking mTORC2 [15,17].”