Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions*
Identifieur interne : 000A28 ( Main/Merge ); précédent : 000A27; suivant : 000A29Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions*
Auteurs : Hedieh Shahpasandzadeh ; Blagovesta Popova ; Alexandra Kleinknecht ; Paul E. Fraser ; Tiago F. Outeiro ; Gerhard H. BrausSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 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
Url:
DOI: 10.1074/jbc.M114.559237
PubMed: 25231978
PubMed Central: 4223324
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PMC:4223324Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions<xref ref-type="fn" rid="FN1">*</xref>
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<author><name sortKey="Shahpasandzadeh, Hedieh" sort="Shahpasandzadeh, Hedieh" uniqKey="Shahpasandzadeh H" first="Hedieh" last="Shahpasandzadeh">Hedieh Shahpasandzadeh</name>
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<series><title level="j">The Journal of Biological Chemistry</title>
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<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>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
Phosphorylation and sumoylation are post-translational modifications of the Parkinson disease protein α-synuclein.</p>
<p><bold>Results:</bold>
α-Synuclein inclusion clearance is impaired in yeast when sumoylation is inhibited; phosphorylation of α-synuclein can compensate SUMO impairment.</p>
<p><bold>Conclusion:</bold>
Sumoylation stimulates autophagy clearance of α-synuclein inclusions, whereas phosphorylation promotes autophagy and proteasome degradation.</p>
<p><bold>Significance:</bold>
A complex molecular post-translational cross-talk is required in yeast to clear toxic inclusions.</p>
</div>
</front>
</TEI>
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