The behavior of α‐synuclein in neurons
Identifieur interne : 001969 ( Main/Exploration ); précédent : 001968; suivant : 001970The behavior of α‐synuclein in neurons
Auteurs : Doris L. Fortin [États-Unis] ; Venu M. Nemani [États-Unis] ; Ken Nakamura [États-Unis] ; Robert H. Edwards [États-Unis]Source :
- Movement Disorders [ 0885-3185 ] ; 2010.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
- Behavior, Calcium (metabolism), Humans, Mobility, Mutation (genetics), Nervous system diseases, Neuron, Neurons (metabolism), Parkinson Disease (genetics), Parkinson Disease (pathology), Parkinson disease, Parkinson's disease, Synaptic vesicle, alpha-Synuclein (genetics), alpha-Synuclein (metabolism), exocytosis, mobility, neuron, synaptic vesicle, α‐synuclein.
- MESH :
- chemical , genetics : alpha-Synuclein.
- chemical , metabolism : Calcium, alpha-Synuclein.
- genetics : Mutation, Parkinson Disease.
- metabolism : Neurons.
- pathology : Parkinson Disease.
- Humans.
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
Url:
DOI: 10.1002/mds.22722
Affiliations:
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Le document en format XML
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Fortin</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Nemani, Venu M" sort="Nemani, Venu M" uniqKey="Nemani V" first="Venu M." last="Nemani">Venu M. 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Edwards</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Movement Disorders</title><title level="j" type="abbrev">Mov. Disord.</title><idno type="ISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2010">2010</date><biblScope unit="vol">25</biblScope><biblScope unit="issue">S1</biblScope><biblScope unit="page" from="S21">S21</biblScope><biblScope unit="page" to="S26">S26</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">BC37776B9C12A3E4CB931F828CBEC5F827C66D9D</idno><idno type="DOI">10.1002/mds.22722</idno><idno type="ArticleID">MDS22722</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Behavior</term><term>Calcium (metabolism)</term><term>Humans</term><term>Mobility</term><term>Mutation (genetics)</term><term>Nervous system diseases</term><term>Neuron</term><term>Neurons (metabolism)</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (pathology)</term><term>Parkinson disease</term><term>Parkinson's disease</term><term>Synaptic vesicle</term><term>alpha-Synuclein (genetics)</term><term>alpha-Synuclein (metabolism)</term><term>exocytosis</term><term>mobility</term><term>neuron</term><term>synaptic vesicle</term><term>α‐synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Comportement</term><term>Maladie de Parkinson</term><term>Mobilité</term><term>Neurone</term><term>Pathologie du système nerveux</term><term>Vésicule synaptique</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Fortin, Doris L" sort="Fortin, Doris L" uniqKey="Fortin D" first="Doris L." last="Fortin">Doris L. Fortin</name></region><name sortKey="Edwards, Robert H" sort="Edwards, Robert H" uniqKey="Edwards R" first="Robert H." last="Edwards">Robert H. 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