Interplay between sumoylation and phosphorylation for protection against α-synuclein inclusions.
Identifieur interne : 000639 ( PubMed/Curation ); précédent : 000638; suivant : 000640Interplay between sumoylation and phosphorylation for protection against α-synuclein inclusions.
Auteurs : Hedieh Shahpasandzadeh [Allemagne] ; Blagovesta Popova [Allemagne] ; Alexandra Kleinknecht [Allemagne] ; Paul E. Fraser [Canada] ; Tiago F. Outeiro [Allemagne] ; Gerhard H. Braus [Allemagne]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2014.
English descriptors
- KwdEn :
- Autophagy, Chromatography, Affinity, G-Protein-Coupled Receptor Kinase 5 (metabolism), Humans, Lewy Bodies (metabolism), Lysine (chemistry), Microscopy, Fluorescence, Phosphorylation, Plasmids (metabolism), Proteasome Endopeptidase Complex (metabolism), Protein Binding, Protein Processing, Post-Translational, Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (metabolism), Sumoylation, Ubiquitin (chemistry), alpha-Synuclein (metabolism).
- MESH :
- chemical , chemistry : Lysine, Ubiquitin.
- chemical , metabolism : G-Protein-Coupled Receptor Kinase 5, Proteasome Endopeptidase Complex, Protein-Serine-Threonine Kinases, alpha-Synuclein.
- metabolism : Lewy Bodies, Plasmids, Saccharomyces cerevisiae.
- Autophagy, Chromatography, Affinity, Humans, Microscopy, Fluorescence, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Sumoylation.
Abstract
Parkinson disease is associated with the progressive loss of dopaminergic neurons from the substantia nigra. The pathological hallmark of the disease is the accumulation of intracytoplasmic inclusions known as Lewy bodies that consist mainly of post-translationally modified forms of α-synuclein. Whereas phosphorylation is one of the major modifications of α-synuclein in Lewy bodies, sumoylation has recently been described. The interplay between α-synuclein phosphorylation and sumoylation is poorly understood. Here, we examined the interplay between these modifications as well as their impact on cell growth and inclusion formation in yeast. We found that α-synuclein is sumoylated in vivo at the same sites in yeast as in human cells. Impaired sumoylation resulted in reduced yeast growth combined with an increased number of cells with inclusions, suggesting that this modification plays a protective role. In addition, inhibition of sumoylation prevented autophagy-mediated aggregate clearance. A defect in α-synuclein sumoylation could be suppressed by serine 129 phosphorylation by the human G protein-coupled receptor kinase 5 (GRK5) in yeast. Phosphorylation reduced foci formation, alleviated yeast growth inhibition, and partially rescued autophagic α-synuclein degradation along with the promotion of proteasomal degradation, resulting in aggregate clearance in the absence of a small ubiquitin-like modifier. These findings suggest a complex interplay between sumoylation and phosphorylation in α-synuclein aggregate clearance, which may open new horizons for the development of therapeutic strategies for Parkinson disease.
DOI: 10.1074/jbc.M114.559237
PubMed: 25231978
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Interplay between sumoylation and phosphorylation for protection against α-synuclein inclusions.</title><author><name sortKey="Shahpasandzadeh, Hedieh" sort="Shahpasandzadeh, Hedieh" uniqKey="Shahpasandzadeh H" first="Hedieh" last="Shahpasandzadeh">Hedieh Shahpasandzadeh</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen</wicri:regionArea></affiliation></author><author><name sortKey="Popova, Blagovesta" sort="Popova, Blagovesta" uniqKey="Popova B" first="Blagovesta" last="Popova">Blagovesta Popova</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen</wicri:regionArea></affiliation></author><author><name sortKey="Kleinknecht, Alexandra" sort="Kleinknecht, Alexandra" uniqKey="Kleinknecht A" first="Alexandra" last="Kleinknecht">Alexandra Kleinknecht</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen</wicri:regionArea></affiliation></author><author><name sortKey="Fraser, Paul E" sort="Fraser, Paul E" uniqKey="Fraser P" first="Paul E" last="Fraser">Paul E. 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Braus</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany, gbraus@gwdg.de.</nlm:affiliation><country wicri:rule="url">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25231978</idno><idno type="pmid">25231978</idno><idno type="doi">10.1074/jbc.M114.559237</idno><idno type="wicri:Area/PubMed/Corpus">000639</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000639</idno><idno type="wicri:Area/PubMed/Curation">000639</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000639</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Interplay between sumoylation and phosphorylation for protection against α-synuclein inclusions.</title><author><name sortKey="Shahpasandzadeh, Hedieh" sort="Shahpasandzadeh, Hedieh" uniqKey="Shahpasandzadeh H" first="Hedieh" last="Shahpasandzadeh">Hedieh Shahpasandzadeh</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen</wicri:regionArea></affiliation></author><author><name sortKey="Popova, Blagovesta" sort="Popova, Blagovesta" uniqKey="Popova B" first="Blagovesta" last="Popova">Blagovesta Popova</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen</wicri:regionArea></affiliation></author><author><name sortKey="Kleinknecht, Alexandra" sort="Kleinknecht, Alexandra" uniqKey="Kleinknecht A" first="Alexandra" last="Kleinknecht">Alexandra Kleinknecht</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen</wicri:regionArea></affiliation></author><author><name sortKey="Fraser, Paul E" sort="Fraser, Paul E" uniqKey="Fraser P" first="Paul E" last="Fraser">Paul E. Fraser</name><affiliation wicri:level="4"><nlm:affiliation>the Tanz Centre for Research in Neurodegenerative Diseases and Department of Medical Biophysics, University of Toronto, Ontario M5T 2S8, Canada, and.</nlm:affiliation><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Outeiro, Tiago F" sort="Outeiro, Tiago F" uniqKey="Outeiro T" first="Tiago F" last="Outeiro">Tiago F. Outeiro</name><affiliation wicri:level="1"><nlm:affiliation>the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany, the Department of Neurodegeneration and Restorative Research, University Medical Center Göttingen, D-37073 Göttingen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany, the Department of Neurodegeneration and Restorative Research, University Medical Center Göttingen, D-37073 Göttingen</wicri:regionArea></affiliation></author><author><name sortKey="Braus, Gerhard H" sort="Braus, Gerhard H" uniqKey="Braus G" first="Gerhard H" last="Braus">Gerhard H. Braus</name><affiliation wicri:level="1"><nlm:affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany, gbraus@gwdg.de.</nlm:affiliation><country wicri:rule="url">Allemagne</country><wicri:regionArea>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany</wicri:regionArea></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy</term><term>Chromatography, Affinity</term><term>G-Protein-Coupled Receptor Kinase 5 (metabolism)</term><term>Humans</term><term>Lewy Bodies (metabolism)</term><term>Lysine (chemistry)</term><term>Microscopy, Fluorescence</term><term>Phosphorylation</term><term>Plasmids (metabolism)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Protein Binding</term><term>Protein Processing, Post-Translational</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Sumoylation</term><term>Ubiquitin (chemistry)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lysine</term><term>Ubiquitin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>G-Protein-Coupled Receptor Kinase 5</term><term>Proteasome Endopeptidase Complex</term><term>Protein-Serine-Threonine Kinases</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lewy Bodies</term><term>Plasmids</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autophagy</term><term>Chromatography, Affinity</term><term>Humans</term><term>Microscopy, Fluorescence</term><term>Phosphorylation</term><term>Protein Binding</term><term>Protein Processing, Post-Translational</term><term>Sumoylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Parkinson disease is associated with the progressive loss of dopaminergic neurons from the substantia nigra. The pathological hallmark of the disease is the accumulation of intracytoplasmic inclusions known as Lewy bodies that consist mainly of post-translationally modified forms of α-synuclein. Whereas phosphorylation is one of the major modifications of α-synuclein in Lewy bodies, sumoylation has recently been described. The interplay between α-synuclein phosphorylation and sumoylation is poorly understood. Here, we examined the interplay between these modifications as well as their impact on cell growth and inclusion formation in yeast. We found that α-synuclein is sumoylated in vivo at the same sites in yeast as in human cells. Impaired sumoylation resulted in reduced yeast growth combined with an increased number of cells with inclusions, suggesting that this modification plays a protective role. In addition, inhibition of sumoylation prevented autophagy-mediated aggregate clearance. A defect in α-synuclein sumoylation could be suppressed by serine 129 phosphorylation by the human G protein-coupled receptor kinase 5 (GRK5) in yeast. Phosphorylation reduced foci formation, alleviated yeast growth inhibition, and partially rescued autophagic α-synuclein degradation along with the promotion of proteasomal degradation, resulting in aggregate clearance in the absence of a small ubiquitin-like modifier. These findings suggest a complex interplay between sumoylation and phosphorylation in α-synuclein aggregate clearance, which may open new horizons for the development of therapeutic strategies for Parkinson disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25231978</PMID><DateCreated><Year>2014</Year><Month>11</Month><Day>08</Day></DateCreated><DateCompleted><Year>2015</Year><Month>01</Month><Day>17</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>289</Volume><Issue>45</Issue><PubDate><Year>2014</Year><Month>Nov</Month><Day>07</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Interplay between sumoylation and phosphorylation for protection against α-synuclein inclusions.</ArticleTitle><Pagination><MedlinePgn>31224-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M114.559237</ELocationID><Abstract><AbstractText>Parkinson disease is associated with the progressive loss of dopaminergic neurons from the substantia nigra. The pathological hallmark of the disease is the accumulation of intracytoplasmic inclusions known as Lewy bodies that consist mainly of post-translationally modified forms of α-synuclein. Whereas phosphorylation is one of the major modifications of α-synuclein in Lewy bodies, sumoylation has recently been described. The interplay between α-synuclein phosphorylation and sumoylation is poorly understood. Here, we examined the interplay between these modifications as well as their impact on cell growth and inclusion formation in yeast. We found that α-synuclein is sumoylated in vivo at the same sites in yeast as in human cells. Impaired sumoylation resulted in reduced yeast growth combined with an increased number of cells with inclusions, suggesting that this modification plays a protective role. In addition, inhibition of sumoylation prevented autophagy-mediated aggregate clearance. A defect in α-synuclein sumoylation could be suppressed by serine 129 phosphorylation by the human G protein-coupled receptor kinase 5 (GRK5) in yeast. Phosphorylation reduced foci formation, alleviated yeast growth inhibition, and partially rescued autophagic α-synuclein degradation along with the promotion of proteasomal degradation, resulting in aggregate clearance in the absence of a small ubiquitin-like modifier. These findings suggest a complex interplay between sumoylation and phosphorylation in α-synuclein aggregate clearance, which may open new horizons for the development of therapeutic strategies for Parkinson disease.</AbstractText><CopyrightInformation>© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shahpasandzadeh</LastName><ForeName>Hedieh</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Popova</LastName><ForeName>Blagovesta</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kleinknecht</LastName><ForeName>Alexandra</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fraser</LastName><ForeName>Paul E</ForeName><Initials>PE</Initials><AffiliationInfo><Affiliation>the Tanz Centre for Research in Neurodegenerative Diseases and Department of Medical Biophysics, University of Toronto, Ontario M5T 2S8, Canada, and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Outeiro</LastName><ForeName>Tiago F</ForeName><Initials>TF</Initials><AffiliationInfo><Affiliation>the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany, the Department of Neurodegeneration and Restorative Research, University Medical Center Göttingen, D-37073 Göttingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Braus</LastName><ForeName>Gerhard H</ForeName><Initials>GH</Initials><AffiliationInfo><Affiliation>From the Institute of Microbiology and Genetics, Department of Molecular Microbiology and Genetics, Georg-August-Universität Göttingen, D-37077 Göttingen, Germany, the Center for Nanoscale Microscopy and Molecular Physiology of the Brain, D-37073 Göttingen, Germany, gbraus@gwdg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>09</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D025801">Ubiquitin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.-</RegistryNumber><NameOfSubstance UI="C496126">PLK2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.16</RegistryNumber><NameOfSubstance UI="D054774">G-Protein-Coupled Receptor Kinase 5</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.16</RegistryNumber><NameOfSubstance UI="C517898">GRK5 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber><NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>K3Z4F929H6</RegistryNumber><NameOfSubstance UI="D008239">Lysine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Genetics. 1989 May;122(1):19-27</RefSource><PMID Version="1">2659436</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Methods Enzymol. 1991;194:1-863</RefSource><PMID Version="1">2005781</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nucleic Acids Res. 1992 Mar 25;20(6):1425</RefSource><PMID 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Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058207" MajorTopicYN="N">Sumoylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025801" MajorTopicYN="N">Ubiquitin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4223324</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Autophagy</Keyword><Keyword MajorTopicYN="N">Post-translational Modification</Keyword><Keyword MajorTopicYN="N">Proteasome</Keyword><Keyword MajorTopicYN="N">Yeast</Keyword><Keyword MajorTopicYN="N">α-Synuclein</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>1</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25231978</ArticleId><ArticleId IdType="pii">M114.559237</ArticleId><ArticleId IdType="doi">10.1074/jbc.M114.559237</ArticleId><ArticleId IdType="pmc">PMC4223324</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour 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