Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 280, Issue 47, Pages 39505-39509Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M506096200
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Funding
- NCI NIH HHS [CA103866] Funding Source: Medline
- NIAID NIH HHS [AI47389] Funding Source: Medline
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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.
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