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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">USP8 and PARK2/parkin-mediated mitophagy </title>
<author><name sortKey="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M" last="Durcan">Thomas M. Durcan</name>
<affiliation><nlm:aff>NONE</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>NONE</nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">25700639</idno>
<idno type="pmc">4502724</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4502724</idno>
<idno type="RBID">PMC:4502724</idno>
<idno type="doi">10.1080/15548627.2015.1009794</idno>
<date when="2015">2015</date>
<idno type="wicri:Area/Pmc/Corpus">000026</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000026</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">USP8 and PARK2/parkin-mediated mitophagy </title>
<author><name sortKey="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M" last="Durcan">Thomas M. Durcan</name>
<affiliation><nlm:aff>NONE</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>NONE</nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">Autophagy</title>
<idno type="ISSN">1554-8627</idno>
<idno type="eISSN">1554-8635</idno>
<imprint><date when="2015">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>The Parkinson disease (PD)-associated E3-ubiquitin (Ub) ligase PARK2/parkin plays a central role in many stress response pathways, and in particular, in mitochondrial quality control. Within this pathway, PARK2 activation is accompanied by a robust increase in its autoubiquitination, followed by clearance of the damaged mitochondria by selective autophagy (mitophagy). Yet, little is known about how this auto-ubiquitination is regulated during mitophagy. In our study, we demonstrate that PARK2 forms predominantly K6-linked Ub conjugates on itself. Moreover, PARK2 interacts with the deubiquitinating enzyme USP8 that preferentially removes these K6-linked conjugates, thereby regulating the activity and function of PARK2 in the pathway. When USP8 is silenced, a persistence of K6-linked Ub conjugates on PARK2 delays both its translocation to damaged mitochondria and successful completion of mitophagy. Taken together, these findings implicate a novel role for K6-linked Ub conjugates and USP8-mediated deubiquitination in the regulation of PARK2 in mitochondrial quality control.</p>
</div>
</front>
</TEI>
<pmc article-type="research-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">Autophagy</journal-id>
<journal-id journal-id-type="iso-abbrev">Autophagy</journal-id>
<journal-id journal-id-type="pmc">KAUP</journal-id>
<journal-title-group><journal-title>Autophagy</journal-title>
</journal-title-group>
<issn pub-type="ppub">1554-8627</issn>
<issn pub-type="epub">1554-8635</issn>
<publisher><publisher-name>Taylor & Francis</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">25700639</article-id>
<article-id pub-id-type="pmc">4502724</article-id>
<article-id pub-id-type="publisher-id">1009794</article-id>
<article-id pub-id-type="doi">10.1080/15548627.2015.1009794</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Autophagic Puncta</subject>
</subj-group>
</article-categories>
<title-group><article-title>USP8 and PARK2/parkin-mediated mitophagy </article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Durcan</surname>
<given-names>Thomas M</given-names>
</name>
<xref ref-type="aff" rid="af0001"><sup>1</sup>
</xref>
<xref ref-type="corresp" rid="an0001"><sup>*</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Fon</surname>
<given-names>Edward A</given-names>
</name>
<xref ref-type="aff" rid="af0001"><sup>1</sup>
</xref>
</contrib>
<aff id="af0001"><label>01</label>
<institution>McGill Parkinson's Program; Department of Neurology and Neurosurgery</institution>
;<institution>Montreal Neurological Institute; McGill University</institution>
; Montreal,<country>Canada</country>
</aff>
</contrib-group>
<author-notes><corresp id="an0001"><label>*</label>
Correspondence to: Thomas M Durcan; Email: <email xlink:href="thomas.durcan@mcgill.ca">thomas.durcan@mcgill.ca</email>
</corresp>
<fn><p>Punctum to: Durcan, TM, Tang, MY, Dashti, EA, Aguileta, MA, Gros, P, Shaler, TA and Fon, EA (2014) USP8 Regulates Mitophagy by Removing K6-linked Ubiquitin Conjugates from Parkin. The EMBO Journal; 33(21): 2473-91.</p>
</fn>
</author-notes>
<pub-date pub-type="epub"><day>20</day>
<month>2</month>
<year>2015</year>
</pub-date>
<pub-date pub-type="collection"><month>2</month>
<year>2015</year>
</pub-date>
<volume>11</volume>
<issue>2</issue>
<fpage seq="22">428</fpage>
<lpage>429</lpage>
<history><date date-type="received"><day>3</day>
<month>12</month>
<year>2014</year>
</date>
<date date-type="rev-recd"><day>8</day>
<month>12</month>
<year>2014</year>
</date>
<date date-type="accepted"><day>9</day>
<month>12</month>
<year>2014</year>
</date>
</history>
<permissions><copyright-statement>© 2015 Taylor & Francis Group, LLC</copyright-statement>
<copyright-year>2015</copyright-year>
<copyright-holder>Taylor & Francis Group, LLC</copyright-holder>
</permissions>
<self-uri content-type="pdf" xlink:href="kaup-11-02-1009794.pdf"></self-uri>
<abstract><p>The Parkinson disease (PD)-associated E3-ubiquitin (Ub) ligase PARK2/parkin plays a central role in many stress response pathways, and in particular, in mitochondrial quality control. Within this pathway, PARK2 activation is accompanied by a robust increase in its autoubiquitination, followed by clearance of the damaged mitochondria by selective autophagy (mitophagy). Yet, little is known about how this auto-ubiquitination is regulated during mitophagy. In our study, we demonstrate that PARK2 forms predominantly K6-linked Ub conjugates on itself. Moreover, PARK2 interacts with the deubiquitinating enzyme USP8 that preferentially removes these K6-linked conjugates, thereby regulating the activity and function of PARK2 in the pathway. When USP8 is silenced, a persistence of K6-linked Ub conjugates on PARK2 delays both its translocation to damaged mitochondria and successful completion of mitophagy. Taken together, these findings implicate a novel role for K6-linked Ub conjugates and USP8-mediated deubiquitination in the regulation of PARK2 in mitochondrial quality control.</p>
</abstract>
<kwd-group kwd-group-type="author"><title>Keywords</title>
<kwd>deubiquitination</kwd>
<kwd>K6 Ub-linkages</kwd>
<kwd>mitophagy</kwd>
<kwd>PARK2/Parkin</kwd>
<kwd>USP8</kwd>
</kwd-group>
<counts><fig-count count="1"></fig-count>
<table-count count="0"></table-count>
<ref-count count="0"></ref-count>
<page-count count="2"></page-count>
</counts>
</article-meta>
</front>
</pmc>
</record>
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