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- W2979332011 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 p97/VCP-dependent mitochondrial extraction of MITOL. These findings imply that ubiquitylation directs peroxisomal translocation of MITOL upon mitophagy stimulation and reveal a novel role for ubiquitin as a sorting signal that allows certain specialized proteins to escape from damaged mitochondria." @default.
- W2979332011 created "2019-10-18" @default.
- W2979332011 creator A5025748633 @default.
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- W2979332011 creator A5081209189 @default.
- W2979332011 date "2019-10-10" @default.
- W2979332011 modified "2023-10-18" @default.
- W2979332011 title "Parkin‐mediated ubiquitylation redistributes MITOL/March5 from mitochondria to peroxisomes" @default.
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- W2979332011 doi "https://doi.org/10.15252/embr.201947728" @default.
- W2979332011 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6893362" @default.
- W2979332011 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31602805" @default.
- W2979332011 hasPublicationYear "2019" @default.
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