Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
Identifieur interne : 001666 ( Ncbi/Merge ); 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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<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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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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<sourceDesc><biblStruct><analytic><title xml:lang="en">Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control.</title>
<author><name sortKey="Mclelland, Gian Luca" sort="Mclelland, Gian Luca" uniqKey="Mclelland G" first="Gian-Luca" last="Mclelland">Gian-Luca Mclelland</name>
<affiliation wicri:level="1"><nlm:affiliation>McGill Parkinson Program Department of Neurology and Neurosurgery, Montreal Neurological Institute and Hospital McGill University, Montreal, QC, Canada.</nlm:affiliation>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>McGill Parkinson Program Department of Neurology and Neurosurgery, Montreal Neurological Institute and Hospital McGill University, Montreal, QC</wicri:regionArea>
<wicri:noRegion>QC</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Soubannier, Vincent" sort="Soubannier, Vincent" uniqKey="Soubannier V" first="Vincent" last="Soubannier">Vincent Soubannier</name>
</author>
<author><name sortKey="Chen, Carol X" sort="Chen, Carol X" uniqKey="Chen C" first="Carol X" last="Chen">Carol X. Chen</name>
</author>
<author><name sortKey="Mcbride, Heidi M" sort="Mcbride, Heidi M" uniqKey="Mcbride H" first="Heidi M" last="Mcbride">Heidi M. Mcbride</name>
</author>
<author><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A" last="Fon">Edward A. Fon</name>
</author>
</analytic>
<series><title level="j">The EMBO journal</title>
<idno type="eISSN">1460-2075</idno>
<imprint><date when="2014" type="published">2014</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antimycin A (pharmacology)</term>
<term>Autophagy (physiology)</term>
<term>Biological Transport</term>
<term>GTP Phosphohydrolases (antagonists & inhibitors)</term>
<term>GTP Phosphohydrolases (genetics)</term>
<term>Genes, Reporter</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Lysosomes (physiology)</term>
<term>Microtubule-Associated Proteins (antagonists & inhibitors)</term>
<term>Microtubule-Associated Proteins (genetics)</term>
<term>Mitochondria (physiology)</term>
<term>Mitochondrial Proteins (antagonists & inhibitors)</term>
<term>Mitochondrial Proteins (genetics)</term>
<term>Mitochondrial Proteins (metabolism)</term>
<term>Models, Biological</term>
<term>Oxidation-Reduction</term>
<term>Oxidative Stress</term>
<term>Parkinson Disease (genetics)</term>
<term>Parkinson Disease (metabolism)</term>
<term>Protein Kinases (physiology)</term>
<term>Proteolysis</term>
<term>RNA Interference</term>
<term>RNA, Small Interfering (pharmacology)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Transport Vesicles (metabolism)</term>
<term>Ubiquitin-Protein Ligases (genetics)</term>
<term>Ubiquitin-Protein Ligases (physiology)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>GTP Phosphohydrolases</term>
<term>Microtubule-Associated Proteins</term>
<term>Mitochondrial Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>GTP Phosphohydrolases</term>
<term>Microtubule-Associated Proteins</term>
<term>Mitochondrial Proteins</term>
<term>Ubiquitin-Protein Ligases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Mitochondrial Proteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antimycin A</term>
<term>RNA, Small Interfering</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Parkinson Disease</term>
<term>Transport Vesicles</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Autophagy</term>
<term>Lysosomes</term>
<term>Mitochondria</term>
<term>Protein Kinases</term>
<term>Ubiquitin-Protein Ligases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Biological Transport</term>
<term>Genes, Reporter</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>Models, Biological</term>
<term>Oxidation-Reduction</term>
<term>Oxidative Stress</term>
<term>Proteolysis</term>
<term>RNA Interference</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Mitochondrial dysfunction has long been associated with Parkinson's disease (PD). Parkin and PINK1, 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.</div>
</front>
</TEI>
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