The behavior of α‐synuclein in neurons
Identifieur interne : 002002 ( Istex/Corpus ); précédent : 002001; suivant : 002003The behavior of α‐synuclein in neurons
Auteurs : Doris L. Fortin ; Venu M. Nemani ; Ken Nakamura ; Robert H. EdwardsSource :
- Movement Disorders [ 0885-3185 ] ; 2010.
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Abstract
Despite considerable evidence linking α‐synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. α‐Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with membranes. To address the dynamics of the protein in live cells, we have used photobleaching and found that α‐synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of α‐synuclein, causing its dispersion from the synapse. In addition to the presumed role of α‐synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease. © 2010 Movement Disorder Society
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DOI: 10.1002/mds.22722
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ISTEX:BC37776B9C12A3E4CB931F828CBEC5F827C66D9DLe document en format XML
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Fortin</name><affiliation><mods:affiliation>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA</mods:affiliation></affiliation></author><author><name sortKey="Nemani, Venu M" sort="Nemani, Venu M" uniqKey="Nemani V" first="Venu M." last="Nemani">Venu M. Nemani</name><affiliation><mods:affiliation>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</mods:affiliation></affiliation></author><author><name sortKey="Nakamura, Ken" sort="Nakamura, Ken" uniqKey="Nakamura K" first="Ken" last="Nakamura">Ken Nakamura</name><affiliation><mods:affiliation>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</mods:affiliation></affiliation></author><author><name sortKey="Edwards, Robert H" sort="Edwards, Robert H" uniqKey="Edwards R" first="Robert H." last="Edwards">Robert H. 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To address the dynamics of the protein in live cells, we have used photobleaching and found that α‐synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of α‐synuclein, causing its dispersion from the synapse. In addition to the presumed role of α‐synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease. © 2010 Movement Disorder Society</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Doris L. Fortin PhD</name><affiliations><json:string>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA</json:string></affiliations></json:item><json:item><name>Venu M. Nemani PhD</name><affiliations><json:string>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</json:string></affiliations></json:item><json:item><name>Ken Nakamura MD, PhD</name><affiliations><json:string>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</json:string></affiliations></json:item><json:item><name>Robert H. 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H.</givenNames><familyName>Edwards</familyName><degrees>MD</degrees></personName><contactDetails><email>edwards@ucsf.edu</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="US" type="organization"><unparsedAffiliation>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="US" type="organization"><unparsedAffiliation>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">α‐synuclein</keyword><keyword xml:id="kwd2">neuron</keyword><keyword xml:id="kwd3">synaptic vesicle</keyword><keyword xml:id="kwd4">mobility</keyword><keyword xml:id="kwd5">exocytosis</keyword><keyword xml:id="kwd6">Parkinson's disease</keyword></keywordGroup><fundingInfo><fundingAgency>National Parkinson Foundation</fundingAgency></fundingInfo><fundingInfo><fundingAgency>NIMH</fundingAgency></fundingInfo><fundingInfo><fundingAgency>NIDA</fundingAgency></fundingInfo><fundingInfo><fundingAgency>NIGMS</fundingAgency></fundingInfo><fundingInfo><fundingAgency>McKnight Foundation</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Hillblom Foundation and Burroughs‐Welcome</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Despite considerable evidence linking α‐synuclein with membranes <i>in vitro</i>, it has proven difficult to demonstrate membrane association of the protein <i>in vivo</i>. α‐Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with membranes. To address the dynamics of the protein in live cells, we have used photobleaching and found that α‐synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of α‐synuclein, causing its dispersion from the synapse. In addition to the presumed role of α‐synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease. © 2010 Movement Disorder Society</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>Potential conflict of interest: None reported.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><!--Version 0.6 générée le 4-12-2015--><mods version="3.6"><titleInfo lang="en"><title>The behavior of α‐synuclein in neurons</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Dynamic Behavior of α‐Synuclein in Neurons</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>The behavior of α‐synuclein in neurons</title></titleInfo><name type="personal"><namePart type="given">Doris L.</namePart><namePart type="family">Fortin</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Venu M.</namePart><namePart type="family">Nemani</namePart><namePart type="termsOfAddress">PhD</namePart><affiliation>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ken</namePart><namePart type="family">Nakamura</namePart><namePart type="termsOfAddress">MD, PhD</namePart><affiliation>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Robert H.</namePart><namePart type="family">Edwards</namePart><namePart type="termsOfAddress">MD</namePart><affiliation>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA</affiliation><description>Correspondence: Departments of Neurology and Physiology, UCSF School of Medicine, 600 16th Street, San Francisco, CA 94158‐2517</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre authority="originalCategForm">article</genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">2010</dateIssued><dateCaptured encoding="w3cdtf">2008-04-03</dateCaptured><dateValid encoding="w3cdtf">2009-07-06</dateValid><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">1</extent><extent unit="references">74</extent><extent unit="words">3828</extent></physicalDescription><abstract lang="en">Despite considerable evidence linking α‐synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. α‐Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with membranes. To address the dynamics of the protein in live cells, we have used photobleaching and found that α‐synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of α‐synuclein, causing its dispersion from the synapse. In addition to the presumed role of α‐synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease. © 2010 Movement Disorder Society</abstract><note type="content">*Potential conflict of interest: None reported.</note><note type="funding">National Parkinson Foundation</note><note type="funding">NIMH</note><note type="funding">NIDA</note><note type="funding">NIGMS</note><note type="funding">McKnight Foundation</note><note type="funding">Hillblom Foundation and Burroughs‐Welcome</note><subject lang="en"><genre>Keywords</genre><topic>α‐synuclein</topic><topic>neuron</topic><topic>synaptic vesicle</topic><topic>mobility</topic><topic>exocytosis</topic><topic>Parkinson's disease</topic></subject><relatedItem type="host"><titleInfo><title>Movement Disorders</title></titleInfo><titleInfo type="abbreviated"><title>Mov. Disord.</title></titleInfo><name type="personal"><namePart type="given">Fahn</namePart><namePart type="family">Stanley</namePart><namePart type="termsOfAddress">MD</namePart></name><name type="personal"><namePart type="given">Marder</namePart><namePart type="family">Karen</namePart><namePart type="termsOfAddress">MD</namePart></name><name type="personal"><namePart type="given">Côté</namePart><namePart type="family">Lucien</namePart><namePart type="termsOfAddress">MD</namePart></name><name type="personal"><namePart type="given">Reich</namePart><namePart type="family">Stephen G.</namePart><namePart type="termsOfAddress">MD</namePart></name><subject><genre>article category</genre><topic>Pathogenesis and Implications for Neuroprotection</topic></subject><identifier type="ISSN">0885-3185</identifier><identifier type="eISSN">1531-8257</identifier><identifier type="DOI">10.1002/(ISSN)1531-8257</identifier><identifier type="PublisherID">MDS</identifier><part><date>2010</date><detail type="title"><title>Frontiers of Science and Clinical Advances in Quality of Life in Parkinson's Disease</title></detail><detail type="volume"><caption>vol.</caption><number>25</number></detail><detail type="issue"><caption>no.</caption><number>S1</number></detail><extent unit="pages"><start>S21</start><end>S26</end><total>6</total></extent></part></relatedItem><identifier type="istex">BC37776B9C12A3E4CB931F828CBEC5F827C66D9D</identifier><identifier type="DOI">10.1002/mds.22722</identifier><identifier type="ArticleID">MDS22722</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2010 Movement Disorder Society</accessCondition><recordInfo><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</recordOrigin><recordContentSource>WILEY</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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