Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme*
Identifieur interne : 000983 ( Pmc/Checkpoint ); précédent : 000982; suivant : 000984Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme*
Auteurs : Thomas M. Durcan ; Maria Kontogiannea ; Nathalie Bedard ; Simon S. Wing ; Edward A. FonSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2011.
Abstract
Url:
DOI: 10.1074/jbc.M111.288449
PubMed: 22081612
PubMed Central: 3249107
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme<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="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M." last="Durcan">Thomas M. Durcan</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Bedard, Nathalie" sort="Bedard, Nathalie" uniqKey="Bedard N" first="Nathalie" last="Bedard">Nathalie Bedard</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Wing, Simon S" sort="Wing, Simon S" uniqKey="Wing S" first="Simon S." last="Wing">Simon S. Wing</name><affiliation><nlm:aff id="aff2"></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="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22081612</idno><idno type="pmc">3249107</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3249107</idno><idno type="RBID">PMC:3249107</idno><idno type="doi">10.1074/jbc.M111.288449</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000562</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000562</idno><idno type="wicri:Area/Pmc/Curation">000562</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000562</idno><idno type="wicri:Area/Pmc/Checkpoint">000983</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000983</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme<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="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M." last="Durcan">Thomas M. Durcan</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Bedard, Nathalie" sort="Bedard, Nathalie" uniqKey="Bedard N" first="Nathalie" last="Bedard">Nathalie Bedard</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Wing, Simon S" sort="Wing, Simon S" uniqKey="Wing S" first="Simon S." last="Wing">Simon S. Wing</name><affiliation><nlm:aff id="aff2"></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="aff1"></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="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> The deubiquitinating enzyme (DUB) ataxin-3 opposes the E3 ubiquitin-ligase activity of parkin, however, the mechanism involved is unclear.</p><p><bold>Results:</bold> Ataxin-3 opposes parkin ubiquitination by regulating the E2 ubiquitin-conjugating enzyme.</p><p><bold>Conclusion:</bold> The components within a E2·E3·DUB complex are functionally coupled to fine-tune the overall extent of ubiquitination.</p><p><bold>Significance:</bold> The work broadens our understanding of the intricate interplay between E3s, DUBs, and the ubiquitination machinery.</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">22081612</article-id><article-id pub-id-type="pmc">3249107</article-id><article-id pub-id-type="publisher-id">M111.288449</article-id><article-id pub-id-type="doi">10.1074/jbc.M111.288449</article-id><article-categories><subj-group subj-group-type="heading"><subject>Molecular Bases of Disease</subject></subj-group></article-categories><title-group><article-title>Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme<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><alt-title alt-title-type="short">Ataxin-3 Regulates Parkin Activity via E2 Enzyme</alt-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="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Kontogiannea</surname><given-names>Maria</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bedard</surname><given-names>Nathalie</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Wing</surname><given-names>Simon S.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref><xref ref-type="author-notes" rid="FN4"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Fon</surname><given-names>Edward A.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="corresp" rid="cor1"><sup>3</sup></xref></contrib><aff id="aff1">From the<label>‡</label>Department of Neurology and Neurosurgery, Centre for Neuronal Survival and McGill Parkinson Program, Montreal Neurological Institute, and</aff><aff id="aff2">the<label>§</label>Department of Medicine, Polypeptide Laboratory, McGill University Health Centre Research Institute, McGill University, Montreal, Quebec H3A 2B4, Canada</aff></contrib-group><author-notes><corresp id="cor1"><label>3</label> Chercheur National of the Fonds de Recherche du Québec-Santé. To whom correspondence should be addressed: <addr-line>Montreal Neurological Institute, Rm. MP036, 3801 University St., Montreal, Quebec H3A 2B4, Canada.</addr-line> Tel.: <phone>514-398-8398</phone>; Fax: <fax>514-398-5214</fax>; E-mail: <email>ted.fon@mcgill.ca</email>.</corresp><fn fn-type="supported-by" id="FN3"><label>1</label><p>Supported by fellowships from the National Ataxia Foundation and the Parkinson's Disease Foundation.</p></fn><fn fn-type="supported-by" id="FN4"><label>2</label><p>Supported by a CIHR Operating Grant MOP-82734.</p></fn></author-notes><pub-date pub-type="ppub"><day>2</day><month>1</month><year>2012</year></pub-date><pub-date pub-type="epub"><day>11</day><month>11</month><year>2011</year></pub-date><volume>287</volume><issue>1</issue><fpage>531</fpage><lpage>541</lpage><history><date date-type="received"><day>4</day><month>8</month><year>2011</year></date><date date-type="rev-recd"><day>9</day><month>11</month><year>2011</year></date></history><permissions><copyright-statement>© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement><copyright-year>2012</copyright-year></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc00112000531.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> The deubiquitinating enzyme (DUB) ataxin-3 opposes the E3 ubiquitin-ligase activity of parkin, however, the mechanism involved is unclear.</p><p><bold>Results:</bold> Ataxin-3 opposes parkin ubiquitination by regulating the E2 ubiquitin-conjugating enzyme.</p><p><bold>Conclusion:</bold> The components within a E2·E3·DUB complex are functionally coupled to fine-tune the overall extent of ubiquitination.</p><p><bold>Significance:</bold> The work broadens our understanding of the intricate interplay between E3s, DUBs, and the ubiquitination machinery.</p></abstract><abstract><p>We reported previously that parkin, a Parkinson disease-associated E3 ubiquitin-ligase interacts with ataxin-3, a deubiquitinating enzyme associated with Machado-Joseph disease. Ataxin-3 was found to counteract parkin self-ubiquitination both <italic>in vitro</italic> and in cells. Moreover, ataxin-3-dependent deubiquitination of parkin required the catalytic cysteine 14 in ataxin-3, although the precise mechanism remained unclear. We report here that ataxin-3 interferes with the attachment of ubiquitin (Ub) onto parkin in real-time during conjugation but is unable to hydrolyze previously assembled parkin-Ub conjugates. The mechanism involves an ataxin-3-dependent stabilization of the complex between parkin and the E2 Ub-conjugating enzyme, which impedes the efficient charging of the E2 with Ub. Moreover, within this complex, the transfer of Ub from the E2 is diverted away from parkin and onto ataxin-3, further explaining how ataxin-3 deubiquitination is coupled to parkin ubiquitination. Taken together, our findings reveal an unexpected convergence upon the E2 Ub-conjugating enzyme in the regulation of an E3/deubiquitinating enzyme pair, with important implications for the function of parkin and ataxin-3, two proteins responsible for closely related neurodegenerative diseases.</p></abstract><kwd-group><kwd>Deubiquitination</kwd><kwd>Parkin</kwd><kwd>Parkinson Disease</kwd><kwd>Ubiquitin</kwd><kwd>Ubiquitin-conjugating Enzyme (Ubc)</kwd><kwd>Ubiquitin Ligase</kwd><kwd>Ataxin-3</kwd><kwd>Machado-Joseph Disease</kwd><kwd>Spinocerebellar Ataxia Type 3</kwd></kwd-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Bedard, Nathalie" sort="Bedard, Nathalie" uniqKey="Bedard N" first="Nathalie" last="Bedard">Nathalie Bedard</name><name sortKey="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M." last="Durcan">Thomas M. Durcan</name><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A." last="Fon">Edward A. Fon</name><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name><name sortKey="Wing, Simon S" sort="Wing, Simon S" uniqKey="Wing S" first="Simon S." last="Wing">Simon S. Wing</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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