Mitophagy, an autophagy-dependent mitochondria-specific degradation pathway conserved from yeast to humans, serves to control the quality and quantity of mitochondria.However,the molecular details underlying this selective clearance process are poorly understood.We have previously established that mitophagy in yeast requires Atg32, a transmembrane protein highly expressed in response to oxidative stress and anchored on the surface of mitochondria.Atg32 interacts with Atg8, a phosphatidylethanolamine (PE)-conjugated ubiquitin-like protein localized to autophagosomes.Mitophagy is partially impaired when the Atg8-Atg32 interaction is reduced, suggesting that Atg8 contributes to degradation of mitochondria via Atg32.