Integrity of mTORC2 is dependent on the rictor Gly-934 site.

摘要: Growth factor signaling coupled to activation of the phosphatidylinositol-3-OH kinase (PI3K)/Akt pathway plays a crucial role in regulation cell proliferation and survival. The key regulatory Akt has been identified as mammalian target rapamycin complex 2 (mTORC2), which functions PI3K-dependent Ser-473 Akt. This is assembled by mTOR its essential components rictor, Sin1 mLST8. recent genetic screening study Caenorhabditis elegans linked specific point mutation rictor an elevated storage fatty acids that resembles deficiency phenotype. In our study, we show cells analogous single (G934E) prevents binding assembly mTORC2, but this does not interfere with rictor-interacting protein Protor. A substitution Gly-934 residue charged amino acid formation rictor/Sin1 heterodimer. expressing G934E mutant remain deficient mTORC2 signaling, detected reduced phosphorylation on low rate. Thus, although full length required interact partner Sin1, controls interaction mTORC2.