TOMM20 is the central receptor component of the translocase of the outer mitochondrial membrane (TOM) complex, essential for recognizing and translocating cytosolically synthesized mitochondrial preproteins across the outer membrane 1. Working with TOMM22, TOMM20 functions as a transit peptide receptor that facilitates preprotein movement into the TOM40 translocation pore 1. TOMM20 plays a critical structural role in mitophagy regulation: it anchors the TOM complex within arrays containing voltage-dependent anion channels (VDAC), enabling stabilization of PINK1 kinase at depolarized mitochondria 1. This TOMM20-mediated PINK1 stabilization triggers downstream mitophagy through recruitment of the E3 ubiquitin ligase PRKN 1. Additionally, TOMM20 participates in mitochondrial quality control through mitochondrial-derived vesicle (MDV) biogenesis, where TOMM20+ MDVs selectively deliver fully assembled β-barrel proteins and the entire TOM import complex to lysosomes for degradation 2. TOMM20 binding capacity also mediates pharmacological interventions: spautin-1 binds TOMM20 to disrupt PINK1 mitochondrial import, promoting PINK1 stabilization and PINK1-PRKN-dependent mitophagy 3. Dysregulation of TOMM20-dependent mitophagy is implicated in neurodegenerative diseases and cancer progression.