Parkin is selectively recruited to dysfunctional mitochondria and promotes their autophagy. Loss-of-function mutations in Park2, the gene coding for the ubiquitin ligase Parkin, are a significant cause of early-onset Parkinson's disease. Parkin's role in maintaining mitochondrial function and integrity is conserved across species. Parkin-null Drosophila exhibit severe phenotypes, including loss of dopaminergic neurons and swollen mitochondria. This study shows that Parkin is selectively recruited to dysfunctional mitochondria with low membrane potential in mammalian cells. After recruitment, Parkin mediates the engulfment of mitochondria by autophagosomes and their subsequent degradation. Parkin is recruited to mitochondria with depolarized membrane potential, as shown by treatment with the mitochondrial uncoupler CCCP. Parkin accumulation on mitochondria is not inhibited by the ATP synthase inhibitor oligomycin, suggesting that reactive oxygen species production is not necessary for Parkin translocation. Parkin's recruitment to mitochondria is also observed in response to mitochondrial damage caused by the pesticide paraquat. Parkin's selective accumulation on depolarized mitochondria is confirmed by fluorescence loss in photobleaching (FLIP) analysis. Parkin promotes the autophagic degradation of damaged mitochondria, which is consistent with the hypothesis that impaired mitochondria are selectively targeted by Parkin. Parkin's role in mitochondrial autophagy (mitophagy) is further supported by the observation that Parkin-deficient cells show reduced mitophagy. Parkin's activity is essential for the autophagic degradation of impaired mitochondria, and its loss leads to the accumulation of dysfunctional mitochondria, contributing to the pathogenesis of Parkinson's disease. Parkin's function in mitochondrial quality control is crucial for maintaining mitochondrial fidelity and preventing neurodegeneration.Parkin is selectively recruited to dysfunctional mitochondria and promotes their autophagy. Loss-of-function mutations in Park2, the gene coding for the ubiquitin ligase Parkin, are a significant cause of early-onset Parkinson's disease. Parkin's role in maintaining mitochondrial function and integrity is conserved across species. Parkin-null Drosophila exhibit severe phenotypes, including loss of dopaminergic neurons and swollen mitochondria. This study shows that Parkin is selectively recruited to dysfunctional mitochondria with low membrane potential in mammalian cells. After recruitment, Parkin mediates the engulfment of mitochondria by autophagosomes and their subsequent degradation. Parkin is recruited to mitochondria with depolarized membrane potential, as shown by treatment with the mitochondrial uncoupler CCCP. Parkin accumulation on mitochondria is not inhibited by the ATP synthase inhibitor oligomycin, suggesting that reactive oxygen species production is not necessary for Parkin translocation. Parkin's recruitment to mitochondria is also observed in response to mitochondrial damage caused by the pesticide paraquat. Parkin's selective accumulation on depolarized mitochondria is confirmed by fluorescence loss in photobleaching (FLIP) analysis. Parkin promotes the autophagic degradation of damaged mitochondria, which is consistent with the hypothesis that impaired mitochondria are selectively targeted by Parkin. Parkin's role in mitochondrial autophagy (mitophagy) is further supported by the observation that Parkin-deficient cells show reduced mitophagy. Parkin's activity is essential for the autophagic degradation of impaired mitochondria, and its loss leads to the accumulation of dysfunctional mitochondria, contributing to the pathogenesis of Parkinson's disease. Parkin's function in mitochondrial quality control is crucial for maintaining mitochondrial fidelity and preventing neurodegeneration.