Ataxin-3 Deubiquitination Is Coupled to Parkin Ubiquitination via E2 Ubiquitin-conjugating Enzyme*
Identifieur interne : 001005 ( Ncbi/Merge ); précédent : 001004; suivant : 001006Ataxin-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.
English descriptors
- KwdEn :
- Animals, Ataxin-3, Catalytic Domain, HEK293 Cells, Humans, Mice, Nuclear Proteins (chemistry), Nuclear Proteins (metabolism), Protein Stability, Transcription Factors (chemistry), Transcription Factors (metabolism), Ubiquitin-Conjugating Enzymes (metabolism), Ubiquitin-Protein Ligases (metabolism), Ubiquitination.
- MESH :
- chemical , chemistry : Nuclear Proteins, Transcription Factors.
- chemical , metabolism : Nuclear Proteins, Transcription Factors, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases.
- chemical : Ataxin-3.
- Animals, Catalytic Domain, HEK293 Cells, Humans, Mice, Protein Stability, Ubiquitination.
Abstract
Url:
DOI: 10.1074/jbc.M111.288449
PubMed: 22081612
PubMed Central: 3249107
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PMC:3249107Le document en format XML
<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><idno type="wicri:source">PubMed</idno><idno type="wicri:Area/PubMed/Corpus">000B12</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000B12</idno><idno type="wicri:Area/PubMed/Curation">000B12</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000B12</idno><idno type="wicri:Area/PubMed/Checkpoint">000B12</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000B12</idno><idno type="wicri:Area/Ncbi/Merge">001005</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><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Ataxin-3</term><term>Catalytic Domain</term><term>HEK293 Cells</term><term>Humans</term><term>Mice</term><term>Nuclear Proteins (chemistry)</term><term>Nuclear Proteins (metabolism)</term><term>Protein Stability</term><term>Transcription Factors (chemistry)</term><term>Transcription Factors (metabolism)</term><term>Ubiquitin-Conjugating Enzymes (metabolism)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nuclear Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nuclear Proteins</term><term>Transcription Factors</term><term>Ubiquitin-Conjugating Enzymes</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Ataxin-3</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Catalytic Domain</term><term>HEK293 Cells</term><term>Humans</term><term>Mice</term><term>Protein Stability</term><term>Ubiquitination</term></keywords></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><double pmid="22081612"><pmc><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><pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Ataxin-3 deubiquitination is coupled to Parkin ubiquitination via E2 ubiquitin-conjugating enzyme.</title><author><name sortKey="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M" last="Durcan">Thomas M. Durcan</name><affiliation wicri:level="1"><nlm:affiliation>Department of Neurology and Neurosurgery, Centre for Neuronal Survival and McGill Parkinson Program, Montreal Neurological Institute, Montreal, Quebec, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Neurology and Neurosurgery, Centre for Neuronal Survival and McGill Parkinson Program, Montreal Neurological Institute, Montreal, Quebec</wicri:regionArea><wicri:noRegion>Quebec</wicri:noRegion></affiliation></author><author><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name></author><author><name sortKey="Bedard, Nathalie" sort="Bedard, Nathalie" uniqKey="Bedard N" first="Nathalie" last="Bedard">Nathalie Bedard</name></author><author><name sortKey="Wing, Simon S" sort="Wing, Simon S" uniqKey="Wing S" first="Simon S" last="Wing">Simon S. Wing</name></author><author><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A" last="Fon">Edward A. Fon</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22081612</idno><idno type="pmid">22081612</idno><idno type="wicri:Area/PubMed/Corpus">000B12</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000B12</idno><idno type="wicri:Area/PubMed/Curation">000B12</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000B12</idno><idno type="wicri:Area/PubMed/Checkpoint">000B12</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000B12</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Ataxin-3 deubiquitination is coupled to Parkin ubiquitination via E2 ubiquitin-conjugating enzyme.</title><author><name sortKey="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M" last="Durcan">Thomas M. Durcan</name><affiliation wicri:level="1"><nlm:affiliation>Department of Neurology and Neurosurgery, Centre for Neuronal Survival and McGill Parkinson Program, Montreal Neurological Institute, Montreal, Quebec, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Neurology and Neurosurgery, Centre for Neuronal Survival and McGill Parkinson Program, Montreal Neurological Institute, Montreal, Quebec</wicri:regionArea><wicri:noRegion>Quebec</wicri:noRegion></affiliation></author><author><name sortKey="Kontogiannea, Maria" sort="Kontogiannea, Maria" uniqKey="Kontogiannea M" first="Maria" last="Kontogiannea">Maria Kontogiannea</name></author><author><name sortKey="Bedard, Nathalie" sort="Bedard, Nathalie" uniqKey="Bedard N" first="Nathalie" last="Bedard">Nathalie Bedard</name></author><author><name sortKey="Wing, Simon S" sort="Wing, Simon S" uniqKey="Wing S" first="Simon S" last="Wing">Simon S. Wing</name></author><author><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A" last="Fon">Edward A. Fon</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Ataxin-3</term><term>Catalytic Domain</term><term>HEK293 Cells</term><term>Humans</term><term>Mice</term><term>Nuclear Proteins (chemistry)</term><term>Nuclear Proteins (metabolism)</term><term>Protein Stability</term><term>Transcription Factors (chemistry)</term><term>Transcription Factors (metabolism)</term><term>Ubiquitin-Conjugating Enzymes (metabolism)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nuclear Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nuclear Proteins</term><term>Transcription Factors</term><term>Ubiquitin-Conjugating Enzymes</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Ataxin-3</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Catalytic Domain</term><term>HEK293 Cells</term><term>Humans</term><term>Mice</term><term>Protein Stability</term><term>Ubiquitination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 in vitro 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.</div></front></TEI></pubmed></double></record>Pour manipuler ce document sous Unix (Dilib)
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