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

  • Koyano F
  • Yamano K
  • Kosako H
  • et al.
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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.

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Koyano, F., Yamano, K., Kosako, H., Kimura, Y., Kimura, M., Fujiki, Y., … Matsuda, N. (2019). Parkin‐mediated ubiquitylation redistributes MITOL/March5 from mitochondria to peroxisomes. EMBO Reports, 20(12). https://doi.org/10.15252/embr.201947728

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