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• W2955542032 abstract "mTORC2 plays critical roles in metabolism, cell survival and actin cytoskeletal dynamics through the phosphorylation of AKT. Despite its importance to biology and medicine, it is unclear how mTORC2-mediated AKT phosphorylation is controlled. Here, we identify an unforeseen principle by which a GDP-bound form of the conserved small G protein Rho GTPase directly activates mTORC2 in AKT phosphorylation in social amoebae (Dictyostelium discoideum) cells. Using biochemical reconstitution with purified proteins, we demonstrate that Rho–GDP promotes AKT phosphorylation by assembling a supercomplex with Ras–GTP and mTORC2. This supercomplex formation is controlled by the chemoattractant-induced phosphorylation of Rho–GDP at S192 by GSK-3. Furthermore, Rho–GDP rescues defects in both mTORC2-mediated AKT phosphorylation and directed cell migration in Rho-null cells in a manner dependent on phosphorylation of S192. Thus, in contrast to the prevailing view that the GDP-bound forms of G proteins are inactive, our study reveals that mTORC2–AKT signalling is activated by Rho–GDP. Senoo et al. show that, in response to chemoattractant stimulation, phosphorylated Rho–GDP in complex with Ras–GTP and mTORC2 promotes AKT phosphorylation to mediate cell migration." @default.
• W2955542032 created "2019-07-12" @default.
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• W2955542032 date "2019-07-01" @default.
• W2955542032 modified "2023-10-18" @default.
• W2955542032 title "Phosphorylated Rho–GDP directly activates mTORC2 kinase towards AKT through dimerization with Ras–GTP to regulate cell migration" @default.
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• W2955542032 doi "https://doi.org/10.1038/s41556-019-0348-8" @default.
• W2955542032 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6650273" @default.
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