Identification of Protein Interfaces between α-Synuclein, the Principal Component of Lewy Bodies in Parkinson Disease, and the Molecular Chaperones Human Hsc70 and the Yeast Ssa1p*
Identifieur interne : 000F45 ( Ncbi/Curation ); précédent : 000F44; suivant : 000F46Identification of Protein Interfaces between α-Synuclein, the Principal Component of Lewy Bodies in Parkinson Disease, and the Molecular Chaperones Human Hsc70 and the Yeast Ssa1p*
Auteurs : Virginie Redeker ; Samantha Pemberton ; Willy Bienvenut [France] ; Luc Bousset ; Ronald MelkiSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2012.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (chemistry), Adenosine Triphosphatases (genetics), Adenosine Triphosphatases (metabolism), HSC70 Heat-Shock Proteins (chemistry), HSC70 Heat-Shock Proteins (genetics), HSC70 Heat-Shock Proteins (metabolism), HSP70 Heat-Shock Proteins (chemistry), HSP70 Heat-Shock Proteins (genetics), HSP70 Heat-Shock Proteins (metabolism), Humans, Lewy Bodies (chemistry), Lewy Bodies (genetics), Lewy Bodies (metabolism), Parkinson Disease (drug therapy), Parkinson Disease (genetics), Parkinson Disease (metabolism), Peptides (chemistry), Peptides (genetics), Peptides (metabolism), Peptides (therapeutic use), Protein Binding, Protein Engineering (methods), Protein Structure, Tertiary, Saccharomyces cerevisiae (chemistry), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Solubility, alpha-Synuclein (chemistry), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , chemistry : Adenosine Triphosphatases, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Peptides, Saccharomyces cerevisiae Proteins, alpha-Synuclein.
- chemical , genetics : Adenosine Triphosphatases, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Peptides, Saccharomyces cerevisiae Proteins, alpha-Synuclein.
- chemical , metabolism : Adenosine Triphosphatases, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Peptides, Saccharomyces cerevisiae Proteins, alpha-Synuclein.
- chemistry : Lewy Bodies, Saccharomyces cerevisiae.
- drug therapy : Parkinson Disease.
- genetics : Lewy Bodies, Parkinson Disease, Saccharomyces cerevisiae.
- metabolism : Lewy Bodies, Parkinson Disease, Saccharomyces cerevisiae.
- methods : Protein Engineering.
- chemical , therapeutic use : Peptides.
- Humans, Protein Binding, Protein Structure, Tertiary, Solubility.
Abstract
Url:
DOI: 10.1074/jbc.M112.387530
PubMed: 22843682
PubMed Central: 3463349
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PMC:3463349Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Identification of Protein Interfaces between α-Synuclein, the Principal Component of Lewy Bodies in Parkinson Disease, and the Molecular Chaperones Human Hsc70 and the Yeast Ssa1p<xref ref-type="fn" rid="FN1">*</xref>
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<author><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name>
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<author><name sortKey="Pemberton, Samantha" sort="Pemberton, Samantha" uniqKey="Pemberton S" first="Samantha" last="Pemberton">Samantha Pemberton</name>
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<author><name sortKey="Bienvenut, Willy" sort="Bienvenut, Willy" uniqKey="Bienvenut W" first="Willy" last="Bienvenut">Willy Bienvenut</name>
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<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (chemistry)</term>
<term>Adenosine Triphosphatases (genetics)</term>
<term>Adenosine Triphosphatases (metabolism)</term>
<term>HSC70 Heat-Shock Proteins (chemistry)</term>
<term>HSC70 Heat-Shock Proteins (genetics)</term>
<term>HSC70 Heat-Shock Proteins (metabolism)</term>
<term>HSP70 Heat-Shock Proteins (chemistry)</term>
<term>HSP70 Heat-Shock Proteins (genetics)</term>
<term>HSP70 Heat-Shock Proteins (metabolism)</term>
<term>Humans</term>
<term>Lewy Bodies (chemistry)</term>
<term>Lewy Bodies (genetics)</term>
<term>Lewy Bodies (metabolism)</term>
<term>Parkinson Disease (drug therapy)</term>
<term>Parkinson Disease (genetics)</term>
<term>Parkinson Disease (metabolism)</term>
<term>Peptides (chemistry)</term>
<term>Peptides (genetics)</term>
<term>Peptides (metabolism)</term>
<term>Peptides (therapeutic use)</term>
<term>Protein Binding</term>
<term>Protein Engineering (methods)</term>
<term>Protein Structure, Tertiary</term>
<term>Saccharomyces cerevisiae (chemistry)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Solubility</term>
<term>alpha-Synuclein (chemistry)</term>
<term>alpha-Synuclein (genetics)</term>
<term>alpha-Synuclein (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Adenosine Triphosphatases</term>
<term>HSC70 Heat-Shock Proteins</term>
<term>HSP70 Heat-Shock Proteins</term>
<term>Peptides</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Adenosine Triphosphatases</term>
<term>HSC70 Heat-Shock Proteins</term>
<term>HSP70 Heat-Shock Proteins</term>
<term>Peptides</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term>
<term>HSC70 Heat-Shock Proteins</term>
<term>HSP70 Heat-Shock Proteins</term>
<term>Peptides</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Lewy Bodies</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Parkinson Disease</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Lewy Bodies</term>
<term>Parkinson Disease</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lewy Bodies</term>
<term>Parkinson Disease</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Protein Engineering</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Peptides</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Humans</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>Solubility</term>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
The mechanism by which molecular chaperones sequester α-synuclein is unknown.</p>
<p><bold>Results:</bold>
We identify the surface interfaces involved in Hsc70 and Ssa1p interaction with α-synuclein.</p>
<p><bold>Conclusion:</bold>
Hsc70 and Ssa1p bind α-synuclein like a tweezer through the two tips of their client protein binding sites.</p>
<p><bold>Significance:</bold>
Elucidating how molecular chaperones bind proteins involved in neurodegenerative diseases is relevant to design therapeutic tools.</p>
</div>
</front>
</TEI>
</record>
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