The study investigates the mechanism by which mitochondrial herniation during apoptosis triggers a unique form of mitophagy, independent of the canonical PINK1/Parkin pathway. During intrinsic apoptosis, BAX/BAK proteins permeabilize the outer mitochondrial membrane (OMM), leading to mitochondrial herniation and exposure of the inner mitochondrial membrane (IMM). This exposure triggers ubiquitination of the IMM, which serves as a signal for autophagy. The ubiquitinated IMM is then targeted for degradation by autophagosomes, delivering damaged mitochondria to lysosomes. This process is independent of STING-induced autophagy and involves recruitment of autophagy adaptors like P62, OPTN, and NDP52 to the herniated mitochondria. The study highlights the importance of IMM-induced mitophagy in containing damaged mitochondria, particularly in situations where caspase activation is incomplete or inhibited, and in contexts where PINK1/Parkin-mitophagy is impaired.The study investigates the mechanism by which mitochondrial herniation during apoptosis triggers a unique form of mitophagy, independent of the canonical PINK1/Parkin pathway. During intrinsic apoptosis, BAX/BAK proteins permeabilize the outer mitochondrial membrane (OMM), leading to mitochondrial herniation and exposure of the inner mitochondrial membrane (IMM). This exposure triggers ubiquitination of the IMM, which serves as a signal for autophagy. The ubiquitinated IMM is then targeted for degradation by autophagosomes, delivering damaged mitochondria to lysosomes. This process is independent of STING-induced autophagy and involves recruitment of autophagy adaptors like P62, OPTN, and NDP52 to the herniated mitochondria. The study highlights the importance of IMM-induced mitophagy in containing damaged mitochondria, particularly in situations where caspase activation is incomplete or inhibited, and in contexts where PINK1/Parkin-mitophagy is impaired.