MovDisordV3, Main, Merge, bibRecord, 002395

The Behavior of α-Synuclein in Neurons

Identifieur interne : 002395 ( Main/Merge ); précédent : 002394; suivant : 002396

The 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.

RBID : Pascal:10-0193442

Descripteurs français

Pascal (Inist)
- Maladie de Parkinson, Pathologie du système nerveux, Comportement, Neurone, Vésicule synaptique, Mobilité.

English descriptors

KwdEn :
- Behavior, Mobility, Nervous system diseases, Neuron, Parkinson disease, Synaptic vesicle.

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.

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Pascal:10-0193442

Le document en format XML

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<author><name sortKey="Edwards, Robert H" sort="Edwards, Robert H" uniqKey="Edwards R" first="Robert H." last="Edwards">Robert H. Edwards</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">The Behavior of α-Synuclein in Neurons</title>
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<series><title level="j" type="main">Movement disorders</title>
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<term>Synaptic vesicle</term>
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<keywords scheme="Pascal" xml:lang="fr"><term>Maladie de Parkinson</term>
<term>Pathologie du   système nerveux</term>
<term>Comportement</term>
<term>Neurone</term>
<term>Vésicule synaptique</term>
<term>Mobilité</term>
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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.</div>
</front>
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<name sortKey="Edwards, Robert H" sort="Edwards, Robert H" uniqKey="Edwards R" first="Robert H." last="Edwards">Robert H. Edwards</name>
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<name sortKey="Nemani, Venu M" sort="Nemani, Venu M" uniqKey="Nemani V" first="Venu M." last="Nemani">Venu M. Nemani</name>
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	Movement Disorders (revue)
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Movement Disorders (revue)

The Behavior of α-Synuclein in Neurons

The Behavior of α-Synuclein in Neurons

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri