Journal
FEBS OPEN BIO
Volume 10, Issue 10, Pages 2149-2156Publisher
WILEY
DOI: 10.1002/2211-5463.12970
Keywords
autophagy; glucose starvation; mTORC1; p70 S6 kinase; protein synthesis
Categories
Funding
- Japan Society for the Promotion of Science (JSPS) [16K01727, 20K11364]
- Descente and Ishimoto Memorial Foundation for the Promotion of Sports Science
- Grants-in-Aid for Scientific Research [16K01727, 20K11364] Funding Source: KAKEN
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Proteolysis is known to play a crucial role in maintaining skeletal muscle mass and function. Autophagy is a conserved intracellular process for the bulk degradation of proteins in lysosomes. Although nutrient starvation is known to induce autophagy, the effect of nutrient repletion following starvation on the mTOR pathway-mediated protein translation remains unclear. In the present study, we examined the effect of glucose starvation on the initiation of protein translation in response to glucose re-addition in C2C12 myotubes. Glucose starvation decreased the phosphorylation of p70 S6 kinase (p70S6K), a bonafide marker for protein translation initiation. Following re-addition of glucose, phosphorylation of p70S6K markedly increased only in glucose-starved cells. Inhibiting autophagy using pharmacological inhibitors diminished the effect of glucose re-addition on the phosphorylation of p70S6K, whereas inhibition of the ubiquitin-proteasome system did not exert any effect. In conclusion, autophagy under glucose starvation partially accounts for the activation of translation initiation by re-addition of glucose.
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