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Autophagic punctum

PRKN regulates inner mitochondrial membrane PHB2 during mitophagy

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Article: 2164643 | Received 23 Dec 2022, Accepted 29 Dec 2022, Published online: 16 Jan 2023

Figures & data

Figure 1. Model for PRKN-mediated ubiquitination on the OMM and IMM during mitophagy. Upon mitochondrial damage, both ubiquitin (UB) and PRKN are phosphorylated by PINK1. OMM proteins are ubiquitinated by PRKN and many ubiquitinated OMM proteins are degraded by proteasomes, leading to OMM rupture. In addition, autophagy receptors (including OPTN) link the ubiquitinated OMM and phagophore (which contains LC3s including LC3B) together. After OMM rupture, the IMM autophagy receptor PHB2 is also ubiquitinated by PRKN, and PRKN-mediated ubiquitination of PHB2 enhances PHB2-LC3 interaction, thereby promoting the phagophore recognition of the “entire” mitochondria during mitophagy.

Figure 1. Model for PRKN-mediated ubiquitination on the OMM and IMM during mitophagy. Upon mitochondrial damage, both ubiquitin (UB) and PRKN are phosphorylated by PINK1. OMM proteins are ubiquitinated by PRKN and many ubiquitinated OMM proteins are degraded by proteasomes, leading to OMM rupture. In addition, autophagy receptors (including OPTN) link the ubiquitinated OMM and phagophore (which contains LC3s including LC3B) together. After OMM rupture, the IMM autophagy receptor PHB2 is also ubiquitinated by PRKN, and PRKN-mediated ubiquitination of PHB2 enhances PHB2-LC3 interaction, thereby promoting the phagophore recognition of the “entire” mitochondria during mitophagy.