Autophagy is a process that recycles intracellular components and eliminates organelles to maintain cellular homeostasis. Mitophagy, a specific form of autophagy that targets mitochondria, has been identified in yeast and mammals. In yeast, mitophagy is mediated by autophagy-related 32 (Atg32), while in mammals, it is mediated by NIP3-like protein X (NIX; also known as BNIP3L). Mitophagy is also regulated by parkin and PTEN-induced putative kinase protein 1 (PINK1) in many metazoan cell types, and mutations in these genes are linked to Parkinson's disease. In yeast, Atg32, a protein anchored in the outer mitochondrial membrane, recruits mitochondria to the isolation membrane and facilitates their degradation. In mammals, NIX, another outer mitochondrial membrane protein, is required for the developmental removal of mitochondria during red blood cell differentiation. NIX binds to the autophagosome marker LC3 and GABARAP, recruiting mitochondria into autophagosomes. PINK1 and parkin play a crucial role in the induction of mitophagy in mammalian cells. PINK1 accumulates on damaged mitochondria, recruiting parkin, which ubiquitylates mitochondrial proteins and promotes their degradation. This process is essential for maintaining mitochondrial quality and regulating their number to meet metabolic demands. Defects in mitophagy, such as mutations in PINK1 and parkin, have been linked to Parkinson's disease. Understanding the mechanisms of mitophagy is crucial for developing treatments for this disease and other conditions related to mitochondrial dysfunction.Autophagy is a process that recycles intracellular components and eliminates organelles to maintain cellular homeostasis. Mitophagy, a specific form of autophagy that targets mitochondria, has been identified in yeast and mammals. In yeast, mitophagy is mediated by autophagy-related 32 (Atg32), while in mammals, it is mediated by NIP3-like protein X (NIX; also known as BNIP3L). Mitophagy is also regulated by parkin and PTEN-induced putative kinase protein 1 (PINK1) in many metazoan cell types, and mutations in these genes are linked to Parkinson's disease. In yeast, Atg32, a protein anchored in the outer mitochondrial membrane, recruits mitochondria to the isolation membrane and facilitates their degradation. In mammals, NIX, another outer mitochondrial membrane protein, is required for the developmental removal of mitochondria during red blood cell differentiation. NIX binds to the autophagosome marker LC3 and GABARAP, recruiting mitochondria into autophagosomes. PINK1 and parkin play a crucial role in the induction of mitophagy in mammalian cells. PINK1 accumulates on damaged mitochondria, recruiting parkin, which ubiquitylates mitochondrial proteins and promotes their degradation. This process is essential for maintaining mitochondrial quality and regulating their number to meet metabolic demands. Defects in mitophagy, such as mutations in PINK1 and parkin, have been linked to Parkinson's disease. Understanding the mechanisms of mitophagy is crucial for developing treatments for this disease and other conditions related to mitochondrial dysfunction.