Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex.
The raptor-mTOR protein complex is a key component of a nutrient-sensitive signaling pathway that regulates cell size by controlling the accumulation of cellular mass. How nutrients regulate signaling through the raptor-mTOR complex is not well known. Here we show that a redox-sensitive mechanism regulates the phosphorylation of the raptor-mTOR effector ... S6K1, the interaction between raptor and mTOR, and the kinase activity of the raptor-mTOR complex. In cells treated with the oxidizing agents diamide or phenylarsine oxide, S6K1 phosphorylation increased and became insensitive to nutrient deprivation. Conversely, the reducing reagent BAL (British anti-Lewisite, also known as 2,3-dimercapto-1-propanol) inhibits S6K1 phosphorylation and stabilizes the interaction of mTOR and raptor to mimic the state of the complex under nutrient-deprived conditions. Our findings suggest that a redox-based signaling mechanism may participate in regulating the nutrient-sensitive raptor-mTOR complex and pathway.
Mesh Terms:
Arsenicals, Cell Line, Diamide, Dimercaprol, Humans, Multiprotein Complexes, Oxidants, Oxidation-Reduction, Phosphorylation, Protein Kinases, Proteins, RNA, Small Interfering, Recombinant Proteins, Ribosomal Protein S6 Kinases, 70-kDa, Signal Transduction, Transfection
Arsenicals, Cell Line, Diamide, Dimercaprol, Humans, Multiprotein Complexes, Oxidants, Oxidation-Reduction, Phosphorylation, Protein Kinases, Proteins, RNA, Small Interfering, Recombinant Proteins, Ribosomal Protein S6 Kinases, 70-kDa, Signal Transduction, Transfection
J. Biol. Chem.
Date: Nov. 25, 2005
PubMed ID: 16183647
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