PINK1 (PTEN-induced kinase 1) is a serine/threonine kinase that functions as a mitochondrial damage sensor, orchestrating cellular responses ranging from cytoprotection to elimination of severely compromised mitochondria 1. Under normal conditions, PINK1 transits through the mitochondrial outer membrane via the TOM complex and is cleaved and released into the cytosol 1. Upon mitochondrial depolarization or stress, PINK1 accumulates at the outer mitochondrial membrane where it phosphorylates polyubiquitin chains at Ser-65, recruiting and activating PARKIN (PRKN) to initiate selective autophagy of damaged mitochondria (mitophagy) 2. PINK1 recruits autophagy receptors NDP52 and optineurin to mitochondria, which then recruit upstream autophagy machinery including ULK1 and WIPI1 2. The PINK1-PRKN pathway also promotes mitochondrial fission through phosphorylation of fission proteins like MFN2 and activation of DNM1L, preventing refusion of damaged mitochondria with healthy networks 3. PINK1 mutations cause early-onset Parkinson's disease 1, and impaired PINK1/PRKN-mediated mitophagy contributes to multiple neurodegenerative disorders including Alzheimer's disease and amyotrophic lateral sclerosis 3. Additionally, PINK1-regulated mitophagy dysfunction is implicated in COPD pathogenesis and hepatocellular carcinoma, suggesting therapeutic potential in modulating this pathway 45.