Autophagy under glucose starvation enhances protein translation initiation in response to re‐addition of glucose in C2C12 myotubes

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.