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 : 000829 ( PubMed/Corpus ); précédent : 000828; suivant : 000830Identification 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 ; Luc Bousset ; Ronald MelkiSource :
- The Journal of biological chemistry [ 1083-351X ] ; 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
Fibrillar α-synuclein (α-Syn) is the principal component of Lewy bodies, which are evident in individuals affected by Parkinson disease (PD). This neuropathologic form of α-Syn plays a central role in PD progression as it has been shown to propagate between neurons. Tools that interfere with α-Syn assembly or change the physicochemical properties of the fibrils have potential therapeutic properties as they may be sufficient to interfere with and/or halt cell-to-cell transmission and the systematic spread of α-Syn assemblies within the central nervous system. Vertebrate molecular chaperones from the constitutive/heat-inducible heat shock protein 70 (Hsc/p70) family have been shown to hinder the assembly of soluble α-Syn into fibrils and to bind to the fibrils and very significantly reduce their toxicity. To understand how Hsc70 family members sequester soluble α-Syn, we set up experiments to identify the molecular chaperone-α-Syn surface interfaces. We cross-linked human Hsc70 and its yeast homologue Ssa1p and α-Syn using a chemical cross-linker and mapped the Hsc70- and Ssa1p-α-Syn interface. We show that the client binding domain of Hsc70 and Ssa1p binds two regions within α-Syn similar to a tweezer, with the first spanning residues 10-45 and the second spanning residues 97-102. Our findings define what is necessary and sufficient for engineering Hsc70- and Ssa1p-derived polypeptide with minichaperone properties with a potential as therapeutic agents in Parkinson disease through their ability to affect α-Syn assembly and/or toxicity.
DOI: 10.1074/jbc.M112.387530
PubMed: 22843682
Links to Exploration step
pubmed:22843682Le document en format XML
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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></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Fibrillar α-synuclein (α-Syn) is the principal component of Lewy bodies, which are evident in individuals affected by Parkinson disease (PD). This neuropathologic form of α-Syn plays a central role in PD progression as it has been shown to propagate between neurons. Tools that interfere with α-Syn assembly or change the physicochemical properties of the fibrils have potential therapeutic properties as they may be sufficient to interfere with and/or halt cell-to-cell transmission and the systematic spread of α-Syn assemblies within the central nervous system. Vertebrate molecular chaperones from the constitutive/heat-inducible heat shock protein 70 (Hsc/p70) family have been shown to hinder the assembly of soluble α-Syn into fibrils and to bind to the fibrils and very significantly reduce their toxicity. To understand how Hsc70 family members sequester soluble α-Syn, we set up experiments to identify the molecular chaperone-α-Syn surface interfaces. We cross-linked human Hsc70 and its yeast homologue Ssa1p and α-Syn using a chemical cross-linker and mapped the Hsc70- and Ssa1p-α-Syn interface. We show that the client binding domain of Hsc70 and Ssa1p binds two regions within α-Syn similar to a tweezer, with the first spanning residues 10-45 and the second spanning residues 97-102. Our findings define what is necessary and sufficient for engineering Hsc70- and Ssa1p-derived polypeptide with minichaperone properties with a potential as therapeutic agents in Parkinson disease through their ability to affect α-Syn assembly and/or toxicity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22843682</PMID><DateCreated><Year>2012</Year><Month>09</Month><Day>24</Day></DateCreated><DateCompleted><Year>2012</Year><Month>12</Month><Day>07</Day></DateCompleted><DateRevised><Year>2015</Year><Month>02</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>287</Volume><Issue>39</Issue><PubDate><Year>2012</Year><Month>Sep</Month><Day>21</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>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.</ArticleTitle><Pagination><MedlinePgn>32630-9</MedlinePgn></Pagination><Abstract><AbstractText>Fibrillar α-synuclein (α-Syn) is the principal component of Lewy bodies, which are evident in individuals affected by Parkinson disease (PD). This neuropathologic form of α-Syn plays a central role in PD progression as it has been shown to propagate between neurons. Tools that interfere with α-Syn assembly or change the physicochemical properties of the fibrils have potential therapeutic properties as they may be sufficient to interfere with and/or halt cell-to-cell transmission and the systematic spread of α-Syn assemblies within the central nervous system. Vertebrate molecular chaperones from the constitutive/heat-inducible heat shock protein 70 (Hsc/p70) family have been shown to hinder the assembly of soluble α-Syn into fibrils and to bind to the fibrils and very significantly reduce their toxicity. To understand how Hsc70 family members sequester soluble α-Syn, we set up experiments to identify the molecular chaperone-α-Syn surface interfaces. We cross-linked human Hsc70 and its yeast homologue Ssa1p and α-Syn using a chemical cross-linker and mapped the Hsc70- and Ssa1p-α-Syn interface. We show that the client binding domain of Hsc70 and Ssa1p binds two regions within α-Syn similar to a tweezer, with the first spanning residues 10-45 and the second spanning residues 97-102. Our findings define what is necessary and sufficient for engineering Hsc70- and Ssa1p-derived polypeptide with minichaperone properties with a potential as therapeutic agents in Parkinson disease through their ability to affect α-Syn assembly and/or toxicity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Redeker</LastName><ForeName>Virginie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pemberton</LastName><ForeName>Samantha</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Bienvenut</LastName><ForeName>Willy</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Bousset</LastName><ForeName>Luc</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Melki</LastName><ForeName>Ronald</ForeName><Initials>R</Initials></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>2012</Year><Month>07</Month><Day>26</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="D050883">HSC70 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018840">HSP70 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C494371">HSPA8 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C497604">SNCA protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.3</RegistryNumber><NameOfSubstance UI="C095973">SSA1 protein, S cerevisiae</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Genetics. 2000 Oct;156(2):501-12</RefSource><PMID 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Version="1">11701329</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050883" MajorTopicYN="N">HSC70 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018840" MajorTopicYN="N">HSP70 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName 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MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000627" MajorTopicYN="N">therapeutic use</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015202" MajorTopicYN="N">Protein Engineering</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces 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