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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A new pathway for mitochondrial quality control: mitochondrial-derived vesicles</title><author><name sortKey="Sugiura, Ayumu" sort="Sugiura, Ayumu" uniqKey="Sugiura A" first="Ayumu" last="Sugiura">Ayumu Sugiura</name><affiliation><nlm:aff id="au1"></nlm:aff></affiliation></author><author><name sortKey="Mclelland, Gian Luca" sort="Mclelland, Gian Luca" uniqKey="Mclelland G" first="Gian-Luca" last="Mclelland">Gian-Luca Mclelland</name><affiliation><nlm:aff id="au1"></nlm:aff></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><nlm:aff id="au1"></nlm:aff></affiliation></author><author><name sortKey="Mcbride, Heidi M" sort="Mcbride, Heidi M" uniqKey="Mcbride H" first="Heidi M" last="Mcbride">Heidi M. Mcbride</name><affiliation><nlm:aff id="au1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25107473</idno><idno type="pmc">4282503</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4282503</idno><idno type="RBID">PMC:4282503</idno><idno type="doi">10.15252/embj.201488104</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000B81</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000B81</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A new pathway for mitochondrial quality control: mitochondrial-derived vesicles</title><author><name sortKey="Sugiura, Ayumu" sort="Sugiura, Ayumu" uniqKey="Sugiura A" first="Ayumu" last="Sugiura">Ayumu Sugiura</name><affiliation><nlm:aff id="au1"></nlm:aff></affiliation></author><author><name sortKey="Mclelland, Gian Luca" sort="Mclelland, Gian Luca" uniqKey="Mclelland G" first="Gian-Luca" last="Mclelland">Gian-Luca Mclelland</name><affiliation><nlm:aff id="au1"></nlm:aff></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><nlm:aff id="au1"></nlm:aff></affiliation></author><author><name sortKey="Mcbride, Heidi M" sort="Mcbride, Heidi M" uniqKey="Mcbride H" first="Heidi M" last="Mcbride">Heidi M. Mcbride</name><affiliation><nlm:aff id="au1"></nlm:aff></affiliation></author></analytic><series><title level="j">The EMBO Journal</title><idno type="ISSN">0261-4189</idno><idno type="eISSN">1460-2075</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The last decade has been marked by tremendous progress in our understanding of the cell biology of mitochondria, with the identification of molecules and mechanisms that regulate their fusion, fission, motility, and the architectural transitions within the inner membrane. More importantly, the manipulation of these machineries in tissues has provided links between mitochondrial dynamics and physiology. Indeed, just as the proteins required for fusion and fission were identified, they were quickly linked to both rare and common human diseases. This highlighted the critical importance of this emerging field to medicine, with new hopes of finding drugable targets for numerous pathologies, from neurodegenerative diseases to inflammation and cancer. In the midst of these exciting new discoveries, an unexpected new aspect of mitochondrial cell biology has been uncovered; the generation of small vesicular carriers that transport mitochondrial proteins and lipids to other intracellular organelles. These mitochondrial-derived vesicles (MDVs) were first found to transport a mitochondrial outer membrane protein MAPL to a subpopulation of peroxisomes. However, other MDVs did not target peroxisomes and instead fused with the late endosome, or multivesicular body. The Parkinson's disease-associated proteins Vps35, Parkin, and PINK1 are involved in the biogenesis of a subset of these MDVs, linking this novel trafficking pathway to human disease. In this review, we outline what has been learned about the mechanisms and functional importance of MDV transport and speculate on the greater impact of these pathways in cellular physiology.</p></div></front></TEI><pmc article-type="review-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">EMBO J</journal-id><journal-id journal-id-type="iso-abbrev">EMBO J</journal-id><journal-id journal-id-type="publisher-id">embj</journal-id><journal-title-group><journal-title>The EMBO Journal</journal-title></journal-title-group><issn pub-type="ppub">0261-4189</issn><issn pub-type="epub">1460-2075</issn><publisher><publisher-name>BlackWell Publishing Ltd</publisher-name><publisher-loc>Oxford, UK</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25107473</article-id><article-id pub-id-type="pmc">4282503</article-id><article-id pub-id-type="doi">10.15252/embj.201488104</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>A new pathway for mitochondrial quality control: mitochondrial-derived vesicles</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Sugiura</surname><given-names>Ayumu</given-names></name><xref ref-type="aff" rid="au1"></xref></contrib><contrib contrib-type="author"><name><surname>McLelland</surname><given-names>Gian-Luca</given-names></name><xref ref-type="aff" rid="au1"></xref></contrib><contrib contrib-type="author"><name><surname>Fon</surname><given-names>Edward A</given-names></name><xref ref-type="aff" rid="au1"></xref></contrib><contrib contrib-type="author"><name><surname>McBride</surname><given-names>Heidi M</given-names></name><xref ref-type="aff" rid="au1"></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff id="au1"><institution>Montreal Neurological Institute, McGill University</institution><addr-line>Montreal, QC, Canada</addr-line></aff></contrib-group><author-notes><corresp id="cor1">*Corresponding author. Tel: +1 514 398 1808; E-mail: <email>heidi.mcbride@mcgill.ca</email></corresp></author-notes><pub-date pub-type="ppub"><day>01</day><month>10</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>08</day><month>8</month><year>2014</year></pub-date><volume>33</volume><issue>19</issue><fpage>2142</fpage><lpage>2156</lpage><history><date date-type="received"><day>03</day><month>2</month><year>2014</year></date><date date-type="rev-recd"><day>08</day><month>7</month><year>2014</year></date><date date-type="accepted"><day>23</day><month>7</month><year>2014</year></date></history><permissions><copyright-statement>© 2014 The Authors</copyright-statement><copyright-year>2014</copyright-year></permissions><abstract><p>The last decade has been marked by tremendous progress in our understanding of the cell biology of mitochondria, with the identification of molecules and mechanisms that regulate their fusion, fission, motility, and the architectural transitions within the inner membrane. More importantly, the manipulation of these machineries in tissues has provided links between mitochondrial dynamics and physiology. Indeed, just as the proteins required for fusion and fission were identified, they were quickly linked to both rare and common human diseases. This highlighted the critical importance of this emerging field to medicine, with new hopes of finding drugable targets for numerous pathologies, from neurodegenerative diseases to inflammation and cancer. In the midst of these exciting new discoveries, an unexpected new aspect of mitochondrial cell biology has been uncovered; the generation of small vesicular carriers that transport mitochondrial proteins and lipids to other intracellular organelles. These mitochondrial-derived vesicles (MDVs) were first found to transport a mitochondrial outer membrane protein MAPL to a subpopulation of peroxisomes. However, other MDVs did not target peroxisomes and instead fused with the late endosome, or multivesicular body. The Parkinson's disease-associated proteins Vps35, Parkin, and PINK1 are involved in the biogenesis of a subset of these MDVs, linking this novel trafficking pathway to human disease. In this review, we outline what has been learned about the mechanisms and functional importance of MDV transport and speculate on the greater impact of these pathways in cellular physiology.</p></abstract><kwd-group><kwd>mitochondria</kwd><kwd>Parkin</kwd><kwd>PINK1</kwd><kwd>quality control</kwd><kwd>vesicle transport</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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