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.
English descriptors
- KwdEn :
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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<front><div type="abstract" xml: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</div>
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<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>
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</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>
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<dateIssued encoding="w3cdtf">2010</dateIssued>
<dateCaptured encoding="w3cdtf">2008-04-03</dateCaptured>
<dateValid encoding="w3cdtf">2009-07-06</dateValid>
<copyrightDate encoding="w3cdtf">2010</copyrightDate>
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<languageTerm type="code" authority="iso639-2b">eng</languageTerm>
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<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>
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<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>
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