Parkin mitochondria in the autophagosome.
Identifieur interne : 000F28 ( PubMed/Checkpoint ); précédent : 000F27; suivant : 000F29Parkin mitochondria in the autophagosome.
Auteurs : Heidi M. Mcbride [Canada]Source :
- The Journal of cell biology [ 1540-8140 ] ; 2008.
English descriptors
- KwdEn :
- Animals, Autophagy (drug effects), Fibroblasts (enzymology), Humans, Membrane Potential, Mitochondrial, Mitochondria (drug effects), Mitochondria (enzymology), Mitochondria (ultrastructure), Neurons (enzymology), Parkinson Disease (enzymology), Parkinson Disease (pathology), Protein Transport, Recombinant Fusion Proteins (metabolism), Signal Transduction, Time Factors, Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism), Uncoupling Agents (pharmacology).
- MESH :
- chemical , genetics : Ubiquitin-Protein Ligases.
- chemical , metabolism : Recombinant Fusion Proteins, Ubiquitin-Protein Ligases.
- drug effects : Autophagy, Mitochondria.
- enzymology : Fibroblasts, Mitochondria, Neurons, Parkinson Disease.
- pathology : Parkinson Disease.
- chemical , pharmacology : Uncoupling Agents.
- ultrastructure : Mitochondria.
- Animals, Humans, Membrane Potential, Mitochondrial, Protein Transport, Signal Transduction, Time Factors.
Abstract
Narendra et al. (see p. 795 of this issue) have made an exciting new discovery that links the fields of mitochondrial quality control and the genetics of Parkinson's disease (PD). Through an elegant series of high-resolution imaging experiments, they are the first to provide evidence that the PARK2 gene product Parkin is selectively recruited to damaged or uncoupled mitochondria. This recruitment leads to the clearance of the organelles through the autophagosome, demonstrating a primary function for Parkin in the regulation of mitochondrial turnover. This work significantly increases our understanding of PD and provides a new framework for the development of therapeutic interventions.
DOI: 10.1083/jcb.200810184
PubMed: 19029341
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:19029341Le document en format XML
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Mcbride</name><affiliation wicri:level="1"><nlm:affiliation>University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7, Canada. hmcbride@ottawaheart.ca</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7</wicri:regionArea><wicri:noRegion>Ontario K1Y 4W7</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:19029341</idno><idno type="pmid">19029341</idno><idno type="doi">10.1083/jcb.200810184</idno><idno type="wicri:Area/PubMed/Corpus">000F29</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000F29</idno><idno type="wicri:Area/PubMed/Curation">000F29</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000F29</idno><idno type="wicri:Area/PubMed/Checkpoint">000F29</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000F29</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Parkin mitochondria in the autophagosome.</title><author><name sortKey="Mcbride, Heidi M" sort="Mcbride, Heidi M" uniqKey="Mcbride H" first="Heidi M" last="Mcbride">Heidi M. Mcbride</name><affiliation wicri:level="1"><nlm:affiliation>University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7, Canada. hmcbride@ottawaheart.ca</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7</wicri:regionArea><wicri:noRegion>Ontario K1Y 4W7</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Journal of cell biology</title><idno type="eISSN">1540-8140</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Autophagy (drug effects)</term><term>Fibroblasts (enzymology)</term><term>Humans</term><term>Membrane Potential, Mitochondrial</term><term>Mitochondria (drug effects)</term><term>Mitochondria (enzymology)</term><term>Mitochondria (ultrastructure)</term><term>Neurons (enzymology)</term><term>Parkinson Disease (enzymology)</term><term>Parkinson Disease (pathology)</term><term>Protein Transport</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Signal Transduction</term><term>Time Factors</term><term>Ubiquitin-Protein Ligases (genetics)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Uncoupling Agents (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Fusion Proteins</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fibroblasts</term><term>Mitochondria</term><term>Neurons</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Uncoupling Agents</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Membrane Potential, Mitochondrial</term><term>Protein Transport</term><term>Signal Transduction</term><term>Time Factors</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Narendra et al. (see p. 795 of this issue) have made an exciting new discovery that links the fields of mitochondrial quality control and the genetics of Parkinson's disease (PD). Through an elegant series of high-resolution imaging experiments, they are the first to provide evidence that the PARK2 gene product Parkin is selectively recruited to damaged or uncoupled mitochondria. This recruitment leads to the clearance of the organelles through the autophagosome, demonstrating a primary function for Parkin in the regulation of mitochondrial turnover. This work significantly increases our understanding of PD and provides a new framework for the development of therapeutic interventions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19029341</PMID><DateCreated><Year>2008</Year><Month>12</Month><Day>02</Day></DateCreated><DateCompleted><Year>2008</Year><Month>12</Month><Day>29</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1540-8140</ISSN><JournalIssue CitedMedium="Internet"><Volume>183</Volume><Issue>5</Issue><PubDate><Year>2008</Year><Month>Dec</Month><Day>01</Day></PubDate></JournalIssue><Title>The Journal of cell biology</Title><ISOAbbreviation>J. Cell Biol.</ISOAbbreviation></Journal><ArticleTitle>Parkin mitochondria in the autophagosome.</ArticleTitle><Pagination><MedlinePgn>757-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1083/jcb.200810184</ELocationID><Abstract><AbstractText>Narendra et al. (see p. 795 of this issue) have made an exciting new discovery that links the fields of mitochondrial quality control and the genetics of Parkinson's disease (PD). Through an elegant series of high-resolution imaging experiments, they are the first to provide evidence that the PARK2 gene product Parkin is selectively recruited to damaged or uncoupled mitochondria. This recruitment leads to the clearance of the organelles through the autophagosome, demonstrating a primary function for Parkin in the regulation of mitochondrial turnover. This work significantly increases our understanding of PD and provides a new framework for the development of therapeutic interventions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>McBride</LastName><ForeName>Heidi M</ForeName><Initials>HM</Initials><AffiliationInfo><Affiliation>University of Ottawa Heart Institute, Ottawa, Ontario K1Y 4W7, Canada. hmcbride@ottawaheart.ca</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="">Comment</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>11</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Cell 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MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005347" MajorTopicYN="N">Fibroblasts</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053078" MajorTopicYN="N">Membrane Potential, Mitochondrial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009474" 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UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014475" MajorTopicYN="N">Uncoupling Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC2592834</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>11</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>12</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>11</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19029341</ArticleId><ArticleId IdType="pii">jcb.200810184</ArticleId><ArticleId 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