α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient.
Identifieur interne : 000279 ( PubMed/Corpus ); précédent : 000278; suivant : 000280α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient.
Auteurs : Amulya Nidhi Shrivastava ; Virginie Redeker ; Nicolas Fritz ; Laura Pieri ; Leandro G. Almeida ; Maria Spolidoro ; Thomas Liebmann ; Luc Bousset ; Marianne Renner ; Clément Léna ; Anita Aperia ; Ronald Melki ; Antoine TrillerSource :
- The EMBO journal [ 1460-2075 ] ; 2015.
English descriptors
- KwdEn :
- Hemiplegia (genetics), Hemiplegia (metabolism), Hemiplegia (pathology), Humans, Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Mutation, Neurons (metabolism), Neurons (pathology), Parkinsonian Disorders (genetics), Parkinsonian Disorders (metabolism), Parkinsonian Disorders (pathology), Sodium-Potassium-Exchanging ATPase (genetics), Sodium-Potassium-Exchanging ATPase (metabolism), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , genetics : Multiprotein Complexes, Sodium-Potassium-Exchanging ATPase, alpha-Synuclein.
- genetics : Hemiplegia, Parkinsonian Disorders.
- metabolism : Hemiplegia, Multiprotein Complexes, Neurons, Parkinsonian Disorders, Sodium-Potassium-Exchanging ATPase, alpha-Synuclein.
- pathology : Hemiplegia, Neurons, Parkinsonian Disorders.
- Humans, Mutation.
Abstract
Extracellular α-synuclein (α-syn) assemblies can be up-taken by neurons; however, their interaction with the plasma membrane and proteins has not been studied specifically. Here we demonstrate that α-syn assemblies form clusters within the plasma membrane of neurons. Using a proteomic-based approach, we identify the α3-subunit of Na+/K+-ATPase (NKA) as a cell surface partner of α-syn assemblies. The interaction strength depended on the state of α-syn, fibrils being the strongest, oligomers weak, and monomers none. Mutations within the neuron-specific α3-subunit are linked to rapid-onset dystonia Parkinsonism (RDP) and alternating hemiplegia of childhood (AHC). We show that freely diffusing α3-NKA are trapped within α-syn clusters resulting in α3-NKA redistribution and formation of larger nanoclusters. This creates regions within the plasma membrane with reduced local densities of α3-NKA, thereby decreasing the efficiency of Na+ extrusion following stimulus. Thus, interactions of α3-NKA with extracellular α-syn assemblies reduce its pumping activity as its mutations in RDP/AHC.
DOI: 10.15252/embj.201591397
PubMed: 26323479
Links to Exploration step
pubmed:26323479Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient.</title><author><name sortKey="Shrivastava, Amulya Nidhi" sort="Shrivastava, Amulya Nidhi" uniqKey="Shrivastava A" first="Amulya Nidhi" last="Shrivastava">Amulya Nidhi Shrivastava</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Redeker, Virginie" sort="Redeker, Virginie" uniqKey="Redeker V" first="Virginie" last="Redeker">Virginie Redeker</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France.</nlm:affiliation></affiliation></author><author><name sortKey="Fritz, Nicolas" sort="Fritz, Nicolas" uniqKey="Fritz N" first="Nicolas" last="Fritz">Nicolas Fritz</name><affiliation><nlm:affiliation>Department of Women and Children's Health, Karolinska Institutet, Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Pieri, Laura" sort="Pieri, Laura" uniqKey="Pieri L" first="Laura" last="Pieri">Laura Pieri</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France.</nlm:affiliation></affiliation></author><author><name sortKey="Almeida, Leandro G" sort="Almeida, Leandro G" uniqKey="Almeida L" first="Leandro G" last="Almeida">Leandro G. 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Almeida</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Spolidoro, Maria" sort="Spolidoro, Maria" uniqKey="Spolidoro M" first="Maria" last="Spolidoro">Maria Spolidoro</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Liebmann, Thomas" sort="Liebmann, Thomas" uniqKey="Liebmann T" first="Thomas" last="Liebmann">Thomas Liebmann</name><affiliation><nlm:affiliation>Department of Women and Children's Health, Karolinska Institutet, Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Bousset, Luc" sort="Bousset, Luc" uniqKey="Bousset L" first="Luc" last="Bousset">Luc Bousset</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France.</nlm:affiliation></affiliation></author><author><name sortKey="Renner, Marianne" sort="Renner, Marianne" uniqKey="Renner M" first="Marianne" last="Renner">Marianne Renner</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Lena, Clement" sort="Lena, Clement" uniqKey="Lena C" first="Clément" last="Léna">Clément Léna</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Aperia, Anita" sort="Aperia, Anita" uniqKey="Aperia A" first="Anita" last="Aperia">Anita Aperia</name><affiliation><nlm:affiliation>Department of Women and Children's Health, Karolinska Institutet, Stockholm, Sweden.</nlm:affiliation></affiliation></author><author><name sortKey="Melki, Ronald" sort="Melki, Ronald" uniqKey="Melki R" first="Ronald" last="Melki">Ronald Melki</name><affiliation><nlm:affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France ronald.melki@lebs.cnrs-gif.fr triller@biologie.ens.fr.</nlm:affiliation></affiliation></author><author><name sortKey="Triller, Antoine" sort="Triller, Antoine" uniqKey="Triller A" first="Antoine" last="Triller">Antoine Triller</name><affiliation><nlm:affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France ronald.melki@lebs.cnrs-gif.fr triller@biologie.ens.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The EMBO journal</title><idno type="eISSN">1460-2075</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Hemiplegia (genetics)</term><term>Hemiplegia (metabolism)</term><term>Hemiplegia (pathology)</term><term>Humans</term><term>Multiprotein Complexes (genetics)</term><term>Multiprotein Complexes (metabolism)</term><term>Mutation</term><term>Neurons (metabolism)</term><term>Neurons (pathology)</term><term>Parkinsonian Disorders (genetics)</term><term>Parkinsonian Disorders (metabolism)</term><term>Parkinsonian Disorders (pathology)</term><term>Sodium-Potassium-Exchanging ATPase (genetics)</term><term>Sodium-Potassium-Exchanging ATPase (metabolism)</term><term>alpha-Synuclein (genetics)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Multiprotein Complexes</term><term>Sodium-Potassium-Exchanging ATPase</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Hemiplegia</term><term>Parkinsonian Disorders</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Hemiplegia</term><term>Multiprotein Complexes</term><term>Neurons</term><term>Parkinsonian Disorders</term><term>Sodium-Potassium-Exchanging ATPase</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Hemiplegia</term><term>Neurons</term><term>Parkinsonian Disorders</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Mutation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Extracellular α-synuclein (α-syn) assemblies can be up-taken by neurons; however, their interaction with the plasma membrane and proteins has not been studied specifically. Here we demonstrate that α-syn assemblies form clusters within the plasma membrane of neurons. Using a proteomic-based approach, we identify the α3-subunit of Na+/K+-ATPase (NKA) as a cell surface partner of α-syn assemblies. The interaction strength depended on the state of α-syn, fibrils being the strongest, oligomers weak, and monomers none. Mutations within the neuron-specific α3-subunit are linked to rapid-onset dystonia Parkinsonism (RDP) and alternating hemiplegia of childhood (AHC). We show that freely diffusing α3-NKA are trapped within α-syn clusters resulting in α3-NKA redistribution and formation of larger nanoclusters. This creates regions within the plasma membrane with reduced local densities of α3-NKA, thereby decreasing the efficiency of Na+ extrusion following stimulus. Thus, interactions of α3-NKA with extracellular α-syn assemblies reduce its pumping activity as its mutations in RDP/AHC.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26323479</PMID><DateCreated><Year>2015</Year><Month>10</Month><Day>02</Day></DateCreated><DateCompleted><Year>2016</Year><Month>01</Month><Day>08</Day></DateCompleted><DateRevised><Year>2016</Year><Month>10</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2075</ISSN><JournalIssue CitedMedium="Internet"><Volume>34</Volume><Issue>19</Issue><PubDate><Year>2015</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J.</ISOAbbreviation></Journal><ArticleTitle>α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradient.</ArticleTitle><Pagination><MedlinePgn>2408-23</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.15252/embj.201591397</ELocationID><Abstract><AbstractText>Extracellular α-synuclein (α-syn) assemblies can be up-taken by neurons; however, their interaction with the plasma membrane and proteins has not been studied specifically. Here we demonstrate that α-syn assemblies form clusters within the plasma membrane of neurons. Using a proteomic-based approach, we identify the α3-subunit of Na+/K+-ATPase (NKA) as a cell surface partner of α-syn assemblies. The interaction strength depended on the state of α-syn, fibrils being the strongest, oligomers weak, and monomers none. Mutations within the neuron-specific α3-subunit are linked to rapid-onset dystonia Parkinsonism (RDP) and alternating hemiplegia of childhood (AHC). We show that freely diffusing α3-NKA are trapped within α-syn clusters resulting in α3-NKA redistribution and formation of larger nanoclusters. This creates regions within the plasma membrane with reduced local densities of α3-NKA, thereby decreasing the efficiency of Na+ extrusion following stimulus. Thus, interactions of α3-NKA with extracellular α-syn assemblies reduce its pumping activity as its mutations in RDP/AHC.</AbstractText><CopyrightInformation>© 2015 The Authors.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shrivastava</LastName><ForeName>Amulya Nidhi</ForeName><Initials>AN</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Redeker</LastName><ForeName>Virginie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fritz</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Women and Children's Health, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pieri</LastName><ForeName>Laura</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Almeida</LastName><ForeName>Leandro G</ForeName><Initials>LG</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Spolidoro</LastName><ForeName>Maria</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liebmann</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Women and Children's Health, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bousset</LastName><ForeName>Luc</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Renner</LastName><ForeName>Marianne</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Léna</LastName><ForeName>Clément</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aperia</LastName><ForeName>Anita</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Women and Children's Health, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Melki</LastName><ForeName>Ronald</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Paris-Saclay Institute of Neuroscience CNRS, Gif-sur-Yvette, France ronald.melki@lebs.cnrs-gif.fr triller@biologie.ens.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Triller</LastName><ForeName>Antoine</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>École Normale Supérieure, Institut de Biologie de l'ENS (IBENS) INSERM CNRS PSL Research University, Paris, France ronald.melki@lebs.cnrs-gif.fr triller@biologie.ens.fr.</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>2015</Year><Month>08</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>EMBO J</MedlineTA><NlmUniqueID>8208664</NlmUniqueID><ISSNLinking>0261-4189</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.3.9</RegistryNumber><NameOfSubstance UI="D000254">Sodium-Potassium-Exchanging ATPase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.3.9</RegistryNumber><NameOfSubstance UI="C552368">sodium potassium ATPase alpha3 subunit, human</NameOfSubstance></Chemical></ChemicalList><SupplMeshList><SupplMeshName Type="Disease" UI="C536589">Alternating hemiplegia of childhood</SupplMeshName></SupplMeshList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Biophys J. 2012 Jun 20;102(12):2894-905</RefSource><PMID Version="1">22735540</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Lancet Neurol. 2012 Sep;11(9):764-73</RefSource><PMID Version="1">22850527</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Neuron. 2004 Jul 22;43(2):169-75</RefSource><PMID Version="1">15260953</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 1986 Apr;83(7):2238-42</RefSource><PMID Version="1">3008155</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Cell. 1993 Jul 2;73(7):1339-47</RefSource><PMID 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Version="1">26373315</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D006429" MajorTopicYN="N">Hemiplegia</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="Y">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020734" MajorTopicYN="N">Parkinsonian Disorders</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000254" MajorTopicYN="N">Sodium-Potassium-Exchanging ATPase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4601662 [Available on 10/01/16]</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">misfolding disease</Keyword><Keyword MajorTopicYN="N">protein aggregation and clustering</Keyword><Keyword MajorTopicYN="N">single particle tracking</Keyword><Keyword MajorTopicYN="N">super‐resolution imaging</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>02</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>07</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>9</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>9</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>1</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26323479</ArticleId><ArticleId IdType="pii">embj.201591397</ArticleId><ArticleId IdType="doi">10.15252/embj.201591397</ArticleId><ArticleId IdType="pmc">PMC4601662</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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