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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<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>
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<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>
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<CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Genetics. 2000 Oct;156(2):501-12</RefSource>
<PMID Version="1">11014801</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>FASEB J. 2011 Jan;25(1):326-36</RefSource>
<PMID Version="1">20876215</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Neurotoxicology. 2002 Oct;23(4-5):527-36</RefSource>
<PMID Version="1">12428725</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Neurobiol Aging. 2003 Mar-Apr;24(2):197-211</RefSource>
<PMID Version="1">12498954</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1131-7</RefSource>
<PMID Version="1">12832755</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2004 Jun 11;279(24):25497-502</RefSource>
<PMID Version="1">15044495</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>JAMA. 1969 Feb 17;207(7):1353-4</RefSource>
<PMID Version="1">5304532</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 1970 Aug 15;227(5259):680-5</RefSource>
<PMID Version="1">5432063</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>JAMA. 1973 Dec 10;226(11):1347-8</RefSource>
<PMID Version="1">4202390</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>JAMA. 1976 May 17;235(20):2217-9</RefSource>
<PMID Version="1">946847</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Anal Biochem. 1976 May 7;72:248-54</RefSource>
<PMID Version="1">942051</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Ann Intern Med. 1977 Mar;86(3):298-300</RefSource>
<PMID Version="1">402877</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 1990 Sep 25;29(38):8921-32</RefSource>
<PMID Version="1">1980210</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 1997 Aug 28;388(6645):839-40</RefSource>
<PMID Version="1">9278044</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2005 Apr 15;280(15):14733-40</RefSource>
<PMID Version="1">15671022</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>FEBS J. 2005 Aug;272(16):4023-33</RefSource>
<PMID Version="1">16098186</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mass Spectrom Rev. 2006 May-Jun;25(3):450-82</RefSource>
<PMID Version="1">16429408</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Proteome Res. 2006 Sep;5(9):2270-82</RefSource>
<PMID Version="1">16944939</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Mol Biol. 2006 Dec 1;364(3):323-36</RefSource>
<PMID Version="1">17010992</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Cell Proteomics. 2007 Dec;6(12):2200-11</RefSource>
<PMID Version="1">17921176</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Parkinsonism Relat Disord. 2007;13 Suppl 3:S309-15</RefSource>
<PMID Version="1">18267256</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Methods. 2008 Apr;5(4):315-8</RefSource>
<PMID Version="1">18327264</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 2008 Nov 25;47(47):12614-25</RefSource>
<PMID Version="1">18975920</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Clin Invest. 2011 Feb;121(2):715-25</RefSource>
<PMID Version="1">21245577</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2011;6(4):e19338</RefSource>
<PMID Version="1">21559417</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2011 Oct 7;286(40):34690-9</RefSource>
<PMID Version="1">21832061</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Neuron. 2011 Oct 6;72(1):57-71</RefSource>
<PMID Version="1">21982369</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2011;6(10):e27230</RefSource>
<PMID Version="1">22073131</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biophys J. 2012 Jun 20;102(12):2894-905</RefSource>
<PMID Version="1">22735540</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Mass Spectrom. 2009 May;44(5):694-706</RefSource>
<PMID Version="1">19132714</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Struct Mol Biol. 2009 Jun;16(6):574-81</RefSource>
<PMID Version="1">19491934</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2009 Aug 4;106(31):13010-5</RefSource>
<PMID Version="1">19651612</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2009 Dec 2;28(23):3758-70</RefSource>
<PMID Version="1">19875982</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biopolymers. 2010 Mar;93(3):218-28</RefSource>
<PMID Version="1">19768775</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Rev Mol Cell Biol. 2010 Apr;11(4):301-7</RefSource>
<PMID Version="1">20308987</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Cell. 2010 Oct 22;40(2):253-66</RefSource>
<PMID Version="1">20965420</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Cold Spring Harb Perspect Biol. 2010 Dec;2(12):a004390</RefSource>
<PMID Version="1">21123396</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>FEBS J. 2010 Dec;277(24):5112-23</RefSource>
<PMID Version="1">21078122</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Trends Biochem Sci. 2001 Nov;26(11):687-9</RefSource>
<PMID Version="1">11701329</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
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