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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Differential Interaction of the E3 Ligase Parkin with the Proteasomal Subunit S5a and the Endocytic Protein Eps15<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Safadi, Susan S" sort="Safadi, Susan S" uniqKey="Safadi S" first="Susan S." last="Safadi">Susan S. Safadi</name><affiliation><nlm:aff id="aff1">From the Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada</nlm:aff></affiliation></author><author><name sortKey="Shaw, Gary S" sort="Shaw, Gary S" uniqKey="Shaw G" first="Gary S." last="Shaw">Gary S. Shaw</name><affiliation><nlm:aff id="aff1">From the Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19875440</idno><idno type="pmc">2801268</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2801268</idno><idno type="RBID">PMC:2801268</idno><idno type="doi">10.1074/jbc.M109.041970</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">000549</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000549</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Differential Interaction of the E3 Ligase Parkin with the Proteasomal Subunit S5a and the Endocytic Protein Eps15<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Safadi, Susan S" sort="Safadi, Susan S" uniqKey="Safadi S" first="Susan S." last="Safadi">Susan S. Safadi</name><affiliation><nlm:aff id="aff1">From the Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada</nlm:aff></affiliation></author><author><name sortKey="Shaw, Gary S" sort="Shaw, Gary S" uniqKey="Shaw G" first="Gary S." last="Shaw">Gary S. Shaw</name><affiliation><nlm:aff id="aff1">From the Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, 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="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Parkin is a multidomain E3 ligase associated with autosomal recessive Parkinson disease. The N-terminal ubiquitin-like domain (Ubld) of parkin functions with the S5a proteasomal subunit, positioning substrate proteins for degradation. In addition the parkin Ubld recruits the endocytotic protein Eps15, allowing the E3 ligase to ubiquinate Eps15 distal from its parkin-interacting site. The recognition sequences in the S5a subunit and Eps15 for the parkin Ubld are ubiquitin-interacting motifs (UIM). Each protein has two UIM sequences separated by a 50-residue spacer in S5a, but only ∼5 residues in Eps15. In this work we used NMR spectroscopy to determine how the parkin Ubld recognizes the proteasomal subunit S5a compared with Eps15, a substrate for ubiquitination. We show that Eps15 contains two flexible α-helices each encompassing a UIM sequence. The α-helix surrounding UIM II is longer than that for UIM I, a situation that is reversed from S5a. Furthermore, we show the parkin Ubld preferentially binds to UIM I in the S5a subunit. This interaction is strongly diminished in a K48A substitution, found near the center of the S5a interacting surface on the parkin Ubld. In contrast to S5a, parkin recruits Eps15 using both its UIM sequences resulting in a larger interaction surface that includes residues from β1 and β2, not typically known to interact with UIM sequences. These results show that the parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.</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="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>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">19875440</article-id><article-id pub-id-type="pmc">2801268</article-id><article-id pub-id-type="publisher-id">M109.041970</article-id><article-id pub-id-type="doi">10.1074/jbc.M109.041970</article-id><article-categories><subj-group subj-group-type="heading"><subject>Protein Structure and Folding</subject></subj-group></article-categories><title-group><article-title>Differential Interaction of the E3 Ligase Parkin with the Proteasomal Subunit S5a and the Endocytic Protein Eps15<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Safadi</surname><given-names>Susan S.</given-names></name><xref ref-type="aff" rid="aff1"></xref></contrib><contrib contrib-type="author"><name><surname>Shaw</surname><given-names>Gary S.</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="corresp" rid="cor1"><sup>1</sup></xref></contrib><aff id="aff1">From the Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada</aff></contrib-group><author-notes><corresp id="cor1"><label>1</label> To whom correspondence should be addressed. Tel.: <phone>519-661-4021</phone>; Fax: <fax>519-661-3175</fax>; E-mail: <email>gshaw1@uwo.ca</email>.</corresp></author-notes><pub-date pub-type="ppub"><day>8</day><month>1</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>29</day><month>10</month><year>2009</year></pub-date><volume>285</volume><issue>2</issue><fpage>1424</fpage><lpage>1434</lpage><history><date date-type="received"><day>7</day><month>7</month><year>2009</year></date><date date-type="rev-recd"><day>22</day><month>10</month><year>2009</year></date></history><permissions><copyright-statement>© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc00210001424.pdf"></self-uri><abstract><p>Parkin is a multidomain E3 ligase associated with autosomal recessive Parkinson disease. The N-terminal ubiquitin-like domain (Ubld) of parkin functions with the S5a proteasomal subunit, positioning substrate proteins for degradation. In addition the parkin Ubld recruits the endocytotic protein Eps15, allowing the E3 ligase to ubiquinate Eps15 distal from its parkin-interacting site. The recognition sequences in the S5a subunit and Eps15 for the parkin Ubld are ubiquitin-interacting motifs (UIM). Each protein has two UIM sequences separated by a 50-residue spacer in S5a, but only ∼5 residues in Eps15. In this work we used NMR spectroscopy to determine how the parkin Ubld recognizes the proteasomal subunit S5a compared with Eps15, a substrate for ubiquitination. We show that Eps15 contains two flexible α-helices each encompassing a UIM sequence. The α-helix surrounding UIM II is longer than that for UIM I, a situation that is reversed from S5a. Furthermore, we show the parkin Ubld preferentially binds to UIM I in the S5a subunit. This interaction is strongly diminished in a K48A substitution, found near the center of the S5a interacting surface on the parkin Ubld. In contrast to S5a, parkin recruits Eps15 using both its UIM sequences resulting in a larger interaction surface that includes residues from β1 and β2, not typically known to interact with UIM sequences. These results show that the parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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