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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Receptor-mediated Endocytosis 8 Utilizes an N-terminal Phosphoinositide-binding Motif to Regulate Endosomal Clathrin Dynamics<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Xhabija, Besa" sort="Xhabija, Besa" uniqKey="Xhabija B" first="Besa" last="Xhabija">Besa Xhabija</name><affiliation><nlm:aff id="aff1">From the Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada</nlm:aff></affiliation></author><author><name sortKey="Vacratsis, Panayiotis O" sort="Vacratsis, Panayiotis O" uniqKey="Vacratsis P" first="Panayiotis O." last="Vacratsis">Panayiotis O. Vacratsis</name><affiliation><nlm:aff id="aff1">From the Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">26134565</idno><idno type="pmc">4571890</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571890</idno><idno type="RBID">PMC:4571890</idno><idno type="doi">10.1074/jbc.M115.644757</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">000038</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000038</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Receptor-mediated Endocytosis 8 Utilizes an N-terminal Phosphoinositide-binding Motif to Regulate Endosomal Clathrin Dynamics<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Xhabija, Besa" sort="Xhabija, Besa" uniqKey="Xhabija B" first="Besa" last="Xhabija">Besa Xhabija</name><affiliation><nlm:aff id="aff1">From the Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada</nlm:aff></affiliation></author><author><name sortKey="Vacratsis, Panayiotis O" sort="Vacratsis, Panayiotis O" uniqKey="Vacratsis P" first="Panayiotis O." last="Vacratsis">Panayiotis O. Vacratsis</name><affiliation><nlm:aff id="aff1">From the Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada</nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</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><bold>Background:</bold> RME-8 is involved in clathrin removal at early endosomes.</p><p><bold>Results:</bold> RME-8 possesses a novel PI(3)P-binding motif within its N terminus.</p><p><bold>Conclusion:</bold> Association of RME-8 with PI(3)P is required for endosomal clathrin removal and alters the steady state localization of retrograde transport cargo CI-MPR.</p><p><bold>Significance:</bold> Regulation of PI(3)P association or PI(3)P levels is likely critical for controlling early endosomal organizational activities.</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">J Biol Chem</journal-id><journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name><publisher-loc>11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">26134565</article-id><article-id pub-id-type="pmc">4571890</article-id><article-id pub-id-type="publisher-id">M115.644757</article-id><article-id pub-id-type="doi">10.1074/jbc.M115.644757</article-id><article-categories><subj-group subj-group-type="heading"><subject>Cell Biology</subject></subj-group></article-categories><title-group><article-title>Receptor-mediated Endocytosis 8 Utilizes an N-terminal Phosphoinositide-binding Motif to Regulate Endosomal Clathrin Dynamics<xref ref-type="fn" rid="FN1">*</xref></article-title><alt-title alt-title-type="short">RME-8 PI(3)P Association Regulates Early Endosomal Clathrin</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Xhabija</surname><given-names>Besa</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="author-notes" rid="FN2"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Vacratsis</surname><given-names>Panayiotis O.</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><aff id="aff1">From the Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada</aff></contrib-group><author-notes><corresp id="cor1"><label>2</label> To whom correspondence should be addressed: <addr-line>Dept. of Chemistry and Biochemistry, University of Windsor, 401 Sunset Ave., Windsor, Ontario N9B 3P4, Canada.</addr-line> Tel.: <phone>519-253-3000 (Ext. 3541)</phone>; E-mail: <email>vacratsi@uwindsor.ca</email>.</corresp><fn fn-type="supported-by" id="FN2"><label>1</label><p>Supported by an Ontario Graduate Scholarship.</p></fn></author-notes><pub-date pub-type="ppub"><day>28</day><month>8</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>1</day><month>7</month><year>2015</year></pub-date><volume>290</volume><issue>35</issue><fpage>21676</fpage><lpage>21689</lpage><history><date date-type="received"><day>11</day><month>2</month><year>2015</year></date><date date-type="rev-recd"><day>25</day><month>6</month><year>2015</year></date></history><permissions><copyright-statement>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement><copyright-year>2015</copyright-year></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc03515021676.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> RME-8 is involved in clathrin removal at early endosomes.</p><p><bold>Results:</bold> RME-8 possesses a novel PI(3)P-binding motif within its N terminus.</p><p><bold>Conclusion:</bold> Association of RME-8 with PI(3)P is required for endosomal clathrin removal and alters the steady state localization of retrograde transport cargo CI-MPR.</p><p><bold>Significance:</bold> Regulation of PI(3)P association or PI(3)P levels is likely critical for controlling early endosomal organizational activities.</p></abstract><abstract><p>Receptor-mediated endocytosis 8 (RME-8) is a DnaJ domain containing protein implicated in translocation of Hsc70 to early endosomes for clathrin removal during retrograde transport. Previously, we have demonstrated that RME-8 associates with early endosomes in a phosphatidylinositol 3-phosphate (PI(3)P)-dependent fashion. In this study, we have now identified amino acid determinants required for PI(3)P binding within a region predicted to adopt a pleckstrin homology-like fold in the N terminus of RME-8. The ability of RME-8 to associate with PI(3)P and early endosomes is largely abolished when residues Lys<sup>17</sup>, Trp<sup>20</sup>, Tyr<sup>24</sup>, or Arg<sup>26</sup> are mutated resulting in diffuse cytoplasmic localization of RME-8 while maintaining the ability to interact with Hsc70. We also provide evidence that RME-8 PI(3)P binding regulates early endosomal clathrin dynamics and alters the steady state localization of the cation-independent mannose 6-phosphate receptor. Interestingly, RME-8 endosomal association is also regulated by the PI(3)P-binding protein SNX1, a member of the retromer complex. Wild type SNX1 restores endosomal localization of RME-8 W20A, whereas a SNX1 variant deficient in PI(3)P binding disrupts endosomal localization of wild type RME-8. These results further highlight the critical role for PI(3)P in the RME-8-mediated organizational control of various endosomal activities, including retrograde transport.</p></abstract><kwd-group><kwd>70-kilodalton heat shock protein (Hsp70)</kwd><kwd>clathrin</kwd><kwd>endocytosis</kwd><kwd>protein motif</kwd><kwd>protein sorting</kwd><kwd>protein-protein interaction</kwd><kwd>PI(3)P</kwd><kwd>RME-8</kwd><kwd>SNX1</kwd><kwd>retrograde transport</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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