2019年12月5日
Parkin‐mediated ubiquitylation redistributes MITOL/March5 from mitochondria to peroxisomes
EMBO reports
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- 巻
- 20
- 号
- 12
- 開始ページ
- e47728
- 終了ページ
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.15252/embr.201947728
- 出版者・発行元
- EMBO
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.
- リンク情報
- ID情報
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- DOI : 10.15252/embr.201947728
- ISSN : 1469-221X
- eISSN : 1469-3178
- PubMed ID : 31602805
- PubMed Central 記事ID : PMC6893362