Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy.
Identifieur interne : 000649 ( PubMed/Checkpoint ); précédent : 000648; suivant : 000650Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy.
Auteurs : Karl Grenier [Canada] ; Maria Kontogiannea [Canada] ; Edward A. Fon [Canada]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2014.
English descriptors
- KwdEn :
- Animals, Cyclin-Dependent Kinase Inhibitor p16 (metabolism), Enzyme Stability, HEK293 Cells, HeLa Cells, Humans, Membrane Potential, Mitochondrial, Mice, Mitochondria (metabolism), Mitochondrial Degradation, Neurons (metabolism), Protein Kinases (metabolism), Protein Transport, Rats, Ubiquitin-Protein Ligases (metabolism).
- MESH :
- chemical , metabolism : Cyclin-Dependent Kinase Inhibitor p16, Protein Kinases, Ubiquitin-Protein Ligases.
- metabolism : Mitochondria, Neurons.
- Animals, Enzyme Stability, HEK293 Cells, HeLa Cells, Humans, Membrane Potential, Mitochondrial, Mice, Mitochondrial Degradation, Protein Transport, Rats.
Abstract
Parkinson disease (PD) is a complex neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra. Multiple genes have been associated with PD, including Parkin and PINK1. Recent studies have established that the Parkin and PINK1 proteins function in a common mitochondrial quality control pathway, whereby disruption of the mitochondrial membrane potential leads to PINK1 stabilization at the mitochondrial outer surface. PINK1 accumulation leads to Parkin recruitment from the cytosol, which in turn promotes the degradation of the damaged mitochondria by autophagy (mitophagy). Most studies characterizing PINK1/Parkin mitophagy have relied on high concentrations of chemical uncouplers to trigger mitochondrial depolarization, a stimulus that has been difficult to adapt to neuronal systems and one unlikely to faithfully model the mitochondrial damage that occurs in PD. Here, we report that the short mitochondrial isoform of ARF (smARF), previously identified as an alternate translation product of the tumor suppressor p19ARF, depolarizes mitochondria and promotes mitophagy in a Parkin/PINK1-dependent manner, both in cell lines and in neurons. The work positions smARF upstream of PINK1 and Parkin and demonstrates that mitophagy can be triggered by intrinsic signaling cascades.
DOI: 10.1074/jbc.M114.607150
PubMed: 25217637
Affiliations:
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Links to Exploration step
pubmed:25217637Le document en format XML
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Fon</name><affiliation wicri:level="4"><nlm:affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.</nlm:affiliation><country wicri:rule="url">Canada</country><wicri:regionArea>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25217637</idno><idno type="pmid">25217637</idno><idno type="doi">10.1074/jbc.M114.607150</idno><idno type="wicri:Area/PubMed/Corpus">000660</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000660</idno><idno type="wicri:Area/PubMed/Curation">000660</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000660</idno><idno type="wicri:Area/PubMed/Checkpoint">000660</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000660</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy.</title><author><name sortKey="Grenier, Karl" sort="Grenier, Karl" uniqKey="Grenier K" first="Karl" last="Grenier">Karl Grenier</name><affiliation wicri:level="4"><nlm:affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author><author><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name><affiliation wicri:level="4"><nlm:affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author><author><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A" last="Fon">Edward A. Fon</name><affiliation wicri:level="4"><nlm:affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.</nlm:affiliation><country wicri:rule="url">Canada</country><wicri:regionArea>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cyclin-Dependent Kinase Inhibitor p16 (metabolism)</term><term>Enzyme Stability</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Membrane Potential, Mitochondrial</term><term>Mice</term><term>Mitochondria (metabolism)</term><term>Mitochondrial Degradation</term><term>Neurons (metabolism)</term><term>Protein Kinases (metabolism)</term><term>Protein Transport</term><term>Rats</term><term>Ubiquitin-Protein Ligases (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cyclin-Dependent Kinase Inhibitor p16</term><term>Protein Kinases</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>Neurons</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Enzyme Stability</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Membrane Potential, Mitochondrial</term><term>Mice</term><term>Mitochondrial Degradation</term><term>Protein Transport</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Parkinson disease (PD) is a complex neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra. Multiple genes have been associated with PD, including Parkin and PINK1. Recent studies have established that the Parkin and PINK1 proteins function in a common mitochondrial quality control pathway, whereby disruption of the mitochondrial membrane potential leads to PINK1 stabilization at the mitochondrial outer surface. PINK1 accumulation leads to Parkin recruitment from the cytosol, which in turn promotes the degradation of the damaged mitochondria by autophagy (mitophagy). Most studies characterizing PINK1/Parkin mitophagy have relied on high concentrations of chemical uncouplers to trigger mitochondrial depolarization, a stimulus that has been difficult to adapt to neuronal systems and one unlikely to faithfully model the mitochondrial damage that occurs in PD. Here, we report that the short mitochondrial isoform of ARF (smARF), previously identified as an alternate translation product of the tumor suppressor p19ARF, depolarizes mitochondria and promotes mitophagy in a Parkin/PINK1-dependent manner, both in cell lines and in neurons. The work positions smARF upstream of PINK1 and Parkin and demonstrates that mitophagy can be triggered by intrinsic signaling cascades.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25217637</PMID><DateCreated><Year>2014</Year><Month>10</Month><Day>25</Day></DateCreated><DateCompleted><Year>2015</Year><Month>02</Month><Day>12</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>289</Volume><Issue>43</Issue><PubDate><Year>2014</Year><Month>Oct</Month><Day>24</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy.</ArticleTitle><Pagination><MedlinePgn>29519-30</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M114.607150</ELocationID><Abstract><AbstractText>Parkinson disease (PD) is a complex neurodegenerative disease characterized by the loss of dopaminergic neurons in the substantia nigra. Multiple genes have been associated with PD, including Parkin and PINK1. Recent studies have established that the Parkin and PINK1 proteins function in a common mitochondrial quality control pathway, whereby disruption of the mitochondrial membrane potential leads to PINK1 stabilization at the mitochondrial outer surface. PINK1 accumulation leads to Parkin recruitment from the cytosol, which in turn promotes the degradation of the damaged mitochondria by autophagy (mitophagy). Most studies characterizing PINK1/Parkin mitophagy have relied on high concentrations of chemical uncouplers to trigger mitochondrial depolarization, a stimulus that has been difficult to adapt to neuronal systems and one unlikely to faithfully model the mitochondrial damage that occurs in PD. Here, we report that the short mitochondrial isoform of ARF (smARF), previously identified as an alternate translation product of the tumor suppressor p19ARF, depolarizes mitochondria and promotes mitophagy in a Parkin/PINK1-dependent manner, both in cell lines and in neurons. The work positions smARF upstream of PINK1 and Parkin and demonstrates that mitophagy can be triggered by intrinsic signaling cascades.</AbstractText><CopyrightInformation>© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Grenier</LastName><ForeName>Karl</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kontogiannea</LastName><ForeName>Maria</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fon</LastName><ForeName>Edward A</ForeName><Initials>EA</Initials><AffiliationInfo><Affiliation>From the Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MOP-62714</GrantID><Agency>Canadian Institutes of Health Research</Agency><Country>Canada</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>09</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol 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Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053078" MajorTopicYN="N">Membrane Potential, Mitochondrial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D063306" MajorTopicYN="Y">Mitochondrial Degradation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4207970</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Mitochondria</Keyword><Keyword MajorTopicYN="N">Mitophagy</Keyword><Keyword MajorTopicYN="N">PTEN-induced Putative Kinase 1 (PINK1)</Keyword><Keyword MajorTopicYN="N">Parkin</Keyword><Keyword MajorTopicYN="N">Parkinson Disease</Keyword><Keyword MajorTopicYN="N">smARF</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>2</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25217637</ArticleId><ArticleId IdType="pii">M114.607150</ArticleId><ArticleId IdType="doi">10.1074/jbc.M114.607150</ArticleId><ArticleId IdType="pmc">PMC4207970</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Québec</li></region><settlement><li>Montréal</li></settlement><orgName><li>Université McGill</li></orgName></list><tree><country name="Canada"><region name="Québec"><name sortKey="Grenier, Karl" sort="Grenier, Karl" uniqKey="Grenier K" first="Karl" last="Grenier">Karl Grenier</name></region><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A" last="Fon">Edward A. Fon</name><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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