Parkin-mediated ubiquitylation redistributes MITOL/March5 from mitochondria to peroxisomes

ABSTRACT: Ubiquitylation of outer mitochondrial membrane (OMM) proteins is closely related to the onset of familial Parkinson's disease. Typically, a reduction in the mitochondrial membrane potential results in Parkin-mediated ubiquitylation of OMM proteins, which are then targeted for proteasomal and mitophagic degradation. The role of ubiquitylation of OMM proteins with non-degradative fates, however, remains poorly understood. In this study, we find that the mitochondrial E3 ubiquitin ligase MITOL/March5 translocates from depolarized mitochondria to peroxisomes following mitophagy stimulation. This unusual redistribution is mediated by peroxins (peroxisomal biogenesis factors) Pex3/16 and requires the E3 ligase activity of Parkin, which ubiquitylates K268 in the MITOL C terminus, essential for p9

SUBMITTER: Ms. Fumika Koyano 

PROVIDER: S-SCDT-EMBOR-2019-47728-T | biostudies-other |

REPOSITORIES: biostudies-other