Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling

By T. Ikenoue, K. Inoki, Qian Yang, Xiaoming Zhou, K. Guan. EMBO Journal, 2008

629 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/2726f8e9f8470f4b10fd383753a3064a9a48b5da

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Citations in the corpus

mTOR: from growth signal integration to cancer, diabetes and ageing (2010, background): “mTORC2 phosphorylates and activates Akt, serum- and glucocorticoid-regulated kinase (SGK), and protein kinase C (PKC), which regulate cell survival, cell cycle progression and anabolism”
Regulation of Immune Responses by mTOR (2011, background): “Finally, protein kinase C alpha (PKCα) is phosphorylated and activated by mTORC2, leading to actin reorganization (47).”
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).”
The nuts and bolts of AGC protein kinases (2010, background): “It is unclear which kinase phosphorylates the turn motif, although phosphorylation of this site is mTORC2 dependen”
A complex interplay between Akt, TSC2, and the two mTOR complexes (2009, background): “While not as severe, these effects on PKCα are similar to that described for MEFs lacking the mTORC2 components Rictor, Sin1, or mLST8 [10,12,13].”
In brief (2011, neutral): “The best-characterized substrates of mTORC1 are S6K and 4E-BP via which mTORC1 controls translation (Sonenberg and Hinnebusch, 2009). mTORC2 consists of mTOR, rictor, mSIN1, mLST8, and PRR5/PRR5L (also known as protor1 and 2) and is insensitive to rapamycin, although long-term rapamycin treatment ca”
Active-Site Inhibitors of mTOR Target Rapamycin-Resistant Outputs of mTORC1 and mTORC2 (2009, background): “Furthermore, PP242 had no effect on the constitutive phosphorylation of the turn motif of Akt at T450 [16,31].”
SREBP Activity Is Regulated by mTORC1 and Contributes to Akt-Dependent Cell Growth (2008, background): “silencing results in reduction of Akt phosphorylation on threonine 450 (Figure S8), which has been shown to be a substrate for mTORC2 (Facchinetti et al., 2008; Ikenoue et al., 2008).”
mTORC1 controls mitochondrial activity and biogenesis through 4E-BP-dependent translational regulation. (2013, background): “, 2012) by activating AGC kinases including serum- and glucocorticoid-regulated kinase (SGK) and AKT (Garcı́a-Martı́nez and Alessi, 2008; Ikenoue et al., 2008; Sarbassov et al., 2005).”