USP8 regulates mitophagy by removing K6-linked ubiquitin conjugates from parkin.
Identifieur interne : 000642 ( PubMed/Corpus ); précédent : 000641; suivant : 000643USP8 regulates mitophagy by removing K6-linked ubiquitin conjugates from parkin.
Auteurs : Thomas M. Durcan ; Matthew Y. Tang ; Joëlle R. Pérusse ; Eman A. Dashti ; Miguel A. Aguileta ; Gian-Luca Mclelland ; Priti Gros ; Thomas A. Shaler ; Denis Faubert ; Benoit Coulombe ; Edward A. FonSource :
- The EMBO journal [ 1460-2075 ] ; 2014.
English descriptors
- KwdEn :
- Endopeptidases (genetics), Endopeptidases (metabolism), Endosomal Sorting Complexes Required for Transport (genetics), Endosomal Sorting Complexes Required for Transport (metabolism), HEK293 Cells, HeLa Cells, Humans, Mitochondria (genetics), Mitochondria (metabolism), Mitochondrial Degradation (physiology), Ubiquitin Thiolesterase (genetics), Ubiquitin Thiolesterase (metabolism), Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism), Ubiquitination (physiology).
- MESH :
- chemical , genetics : Endopeptidases, Endosomal Sorting Complexes Required for Transport, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases.
- chemical , metabolism : Endopeptidases, Endosomal Sorting Complexes Required for Transport, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases.
- genetics : Mitochondria.
- metabolism : Mitochondria.
- physiology : Mitochondrial Degradation, Ubiquitination.
- HEK293 Cells, HeLa Cells, Humans.
Abstract
Mutations in the Park2 gene, encoding the E3 ubiquitin-ligase parkin, are responsible for a familial form of Parkinson's disease (PD). Parkin-mediated ubiquitination is critical for the efficient elimination of depolarized dysfunctional mitochondria by autophagy (mitophagy). As damaged mitochondria are a major source of toxic reactive oxygen species within the cell, this pathway is believed to be highly relevant to the pathogenesis of PD. Little is known about how parkin-mediated ubiquitination is regulated during mitophagy or about the nature of the ubiquitin conjugates involved. We report here that USP8/UBPY, a deubiquitinating enzyme not previously implicated in mitochondrial quality control, is critical for parkin-mediated mitophagy. USP8 preferentially removes non-canonical K6-linked ubiquitin chains from parkin, a process required for the efficient recruitment of parkin to depolarized mitochondria and for their subsequent elimination by mitophagy. This work uncovers a novel role for USP8-mediated deubiquitination of K6-linked ubiquitin conjugates from parkin in mitochondrial quality control.
DOI: 10.15252/embj.201489729
PubMed: 25216678
Links to Exploration step
pubmed:25216678Le document en format XML
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<front><div type="abstract" xml:lang="en">Mutations in the Park2 gene, encoding the E3 ubiquitin-ligase parkin, are responsible for a familial form of Parkinson's disease (PD). Parkin-mediated ubiquitination is critical for the efficient elimination of depolarized dysfunctional mitochondria by autophagy (mitophagy). As damaged mitochondria are a major source of toxic reactive oxygen species within the cell, this pathway is believed to be highly relevant to the pathogenesis of PD. Little is known about how parkin-mediated ubiquitination is regulated during mitophagy or about the nature of the ubiquitin conjugates involved. We report here that USP8/UBPY, a deubiquitinating enzyme not previously implicated in mitochondrial quality control, is critical for parkin-mediated mitophagy. USP8 preferentially removes non-canonical K6-linked ubiquitin chains from parkin, a process required for the efficient recruitment of parkin to depolarized mitochondria and for their subsequent elimination by mitophagy. This work uncovers a novel role for USP8-mediated deubiquitination of K6-linked ubiquitin conjugates from parkin in mitochondrial quality control.</div>
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<Abstract><AbstractText>Mutations in the Park2 gene, encoding the E3 ubiquitin-ligase parkin, are responsible for a familial form of Parkinson's disease (PD). Parkin-mediated ubiquitination is critical for the efficient elimination of depolarized dysfunctional mitochondria by autophagy (mitophagy). As damaged mitochondria are a major source of toxic reactive oxygen species within the cell, this pathway is believed to be highly relevant to the pathogenesis of PD. Little is known about how parkin-mediated ubiquitination is regulated during mitophagy or about the nature of the ubiquitin conjugates involved. We report here that USP8/UBPY, a deubiquitinating enzyme not previously implicated in mitochondrial quality control, is critical for parkin-mediated mitophagy. USP8 preferentially removes non-canonical K6-linked ubiquitin chains from parkin, a process required for the efficient recruitment of parkin to depolarized mitochondria and for their subsequent elimination by mitophagy. This work uncovers a novel role for USP8-mediated deubiquitination of K6-linked ubiquitin conjugates from parkin in mitochondrial quality control.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Durcan</LastName>
<ForeName>Thomas M</ForeName>
<Initials>TM</Initials>
<AffiliationInfo><Affiliation>McGill Parkinson Program, Department of Neurology & Neurosurgery, Montreal Neurological Institute, McGill University, Montréal, QC, Canada.</Affiliation>
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<Author ValidYN="Y"><LastName>Tang</LastName>
<ForeName>Matthew Y</ForeName>
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