Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
Identifieur interne : 001666 ( Ncbi/Curation ); précédent : 001665; suivant : 001667Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
Auteurs : Gian-Luca Mclelland [Canada] ; Vincent Soubannier [Canada] ; Carol X. Chen [Canada] ; Heidi M. Mcbride [Canada] ; Edward A. Fon [Canada]Source :
- The EMBO Journal [ 0261-4189 ] ; 2014.
English descriptors
- KwdEn :
- Antimycin A (pharmacology), Autophagy (physiology), Biological Transport, GTP Phosphohydrolases (antagonists & inhibitors), GTP Phosphohydrolases (genetics), Genes, Reporter, HeLa Cells, Humans, Lysosomes (physiology), Microtubule-Associated Proteins (antagonists & inhibitors), Microtubule-Associated Proteins (genetics), Mitochondria (physiology), Mitochondrial Proteins (antagonists & inhibitors), Mitochondrial Proteins (genetics), Mitochondrial Proteins (metabolism), Models, Biological, Oxidation-Reduction, Oxidative Stress, Parkinson Disease (genetics), Parkinson Disease (metabolism), Protein Kinases (physiology), Proteolysis, RNA Interference, RNA, Small Interfering (pharmacology), Recombinant Fusion Proteins (metabolism), Transport Vesicles (metabolism), Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (physiology).
- MESH :
- chemical , antagonists & inhibitors : GTP Phosphohydrolases, Microtubule-Associated Proteins, Mitochondrial Proteins.
- chemical , genetics : GTP Phosphohydrolases, Microtubule-Associated Proteins, Mitochondrial Proteins, Ubiquitin-Protein Ligases.
- chemical , metabolism : Mitochondrial Proteins, Recombinant Fusion Proteins.
- chemical , pharmacology : Antimycin A, RNA, Small Interfering.
- genetics : Parkinson Disease.
- metabolism : Parkinson Disease, Transport Vesicles.
- physiology : Autophagy, Lysosomes, Mitochondria, Protein Kinases, Ubiquitin-Protein Ligases.
- Biological Transport, Genes, Reporter, HeLa Cells, Humans, Models, Biological, Oxidation-Reduction, Oxidative Stress, Proteolysis, RNA Interference.
Abstract
Mitochondrial dysfunction has long been associated with Parkinson's disease (PD).
Url:
DOI: 10.1002/embj.201385902
PubMed: 24446486
PubMed Central: 3989637
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PMC:3989637Le document en format XML
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<term>GTP Phosphohydrolases (genetics)</term>
<term>Genes, Reporter</term>
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<term>Parkinson Disease (metabolism)</term>
<term>Protein Kinases (physiology)</term>
<term>Proteolysis</term>
<term>RNA Interference</term>
<term>RNA, Small Interfering (pharmacology)</term>
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<term>Transport Vesicles (metabolism)</term>
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<term>Ubiquitin-Protein Ligases (physiology)</term>
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<term>Mitochondrial Proteins</term>
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<term>Microtubule-Associated Proteins</term>
<term>Mitochondrial Proteins</term>
<term>Ubiquitin-Protein Ligases</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Mitochondrial Proteins</term>
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<term>Genes, Reporter</term>
<term>HeLa Cells</term>
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<front><div type="abstract" xml:lang="en"><p>Mitochondrial dysfunction has long been associated with Parkinson's disease (PD). <italic>Parkin</italic>
and <italic>PINK1</italic>
, two genes associated with familial PD, have been implicated in the degradation of depolarized mitochondria via autophagy (mitophagy). Here, we describe the involvement of parkin and PINK1 in a vesicular pathway regulating mitochondrial quality control. This pathway is distinct from canonical mitophagy and is triggered by the generation of oxidative stress from within mitochondria. Wild-type but not PD-linked mutant parkin supports the biogenesis of a population of mitochondria-derived vesicles (MDVs), which bud off mitochondria and contain a specific repertoire of cargo proteins. These MDVs require PINK1 expression and ultimately target to lysosomes for degradation. We hypothesize that loss of this parkin- and PINK1-dependent trafficking mechanism impairs the ability of mitochondria to selectively degrade oxidized and damaged proteins leading, over time, to the mitochondrial dysfunction noted in PD.</p>
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