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Additional info for Structure, Function and Regulation of TOR complexes from Yeasts to Mammals: Part A
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Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 110:177–189. 7. A. (2003). LST8 negatively regulates amino acid biosynthesis as a component of the TOR pathway. J Cell Biol 161:333–347. 8. , et al. (2003). GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol Cell 11:895–904. 9. , et al. (2004). Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton.
33. , and Xu, T. (2002). Akt regulates growth by directly phosphorylating Tsc2. Nat Cell Biol 4:658–665. 34. B. (2002). Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake. Mol Biol Cell 13:2276–2288. 35. , et al. (2007). The proline-rich Akt substrate of 40 kDa (PRAS40) is a physiological substrate of mammalian target of rapamycin complex 1. J Biol Chem 282:20329–20339. 36. , Jr (2007). PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding.
As DEPTOR functions as an inhibitor of both mTORC1 and mTORC2, it might be predicted that overexpression of DEPTOR would shut down all mTOR signaling. Interestingly, this is not the case, and overexpression of DEPTOR actually leads to increased mTORC2 signaling and the activation of Akt. DEPTOR has 13 serine and threonine phosphorylation sites, and DEPTOR is phosphorylated in an mTOR-dependent manner. Work with a nonphosphorylatable DEPTOR mutant indicates that phosphorylated DEPTOR binds preferentially to mTORC1, and that phosphorylation of DEPTOR reverses the inhibitory effects of DEPTOR on mTORC2 activity.