The behavior of alpha-synuclein in neurons.
Identifieur interne : 002A63 ( Ncbi/Checkpoint ); précédent : 002A62; suivant : 002A64The behavior of alpha-synuclein in neurons.
Auteurs : Doris L. Fortin [États-Unis] ; Venu M. Nemani ; Ken Nakamura ; Robert H. EdwardsSource :
- Movement disorders : official journal of the Movement Disorder Society [ 1531-8257 ] ; 2010.
English descriptors
- KwdEn :
- 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 alpha-synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. alpha-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 alpha-synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of alpha-synuclein, causing its dispersion from the synapse. In addition to the presumed role of alpha-synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease.
DOI: 10.1002/mds.22722
PubMed: 20187244
Affiliations:
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pubmed:20187244Le document en format XML
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<affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
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<author><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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<author><name sortKey="Nakamura, Ken" sort="Nakamura, Ken" uniqKey="Nakamura K" first="Ken" last="Nakamura">Ken Nakamura</name>
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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">The behavior of alpha-synuclein in neurons.</title>
<author><name sortKey="Fortin, Doris L" sort="Fortin, Doris L" uniqKey="Fortin D" first="Doris L" last="Fortin">Doris L. Fortin</name>
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<author><name sortKey="Nakamura, Ken" sort="Nakamura, Ken" uniqKey="Nakamura K" first="Ken" last="Nakamura">Ken Nakamura</name>
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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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<series><title level="j">Movement disorders : official journal of the Movement Disorder Society</title>
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<term>Mutation (genetics)</term>
<term>Neurons (metabolism)</term>
<term>Parkinson Disease (genetics)</term>
<term>Parkinson Disease (pathology)</term>
<term>alpha-Synuclein (genetics)</term>
<term>alpha-Synuclein (metabolism)</term>
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<front><div type="abstract" xml:lang="en">Despite considerable evidence linking alpha-synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. alpha-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 alpha-synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of alpha-synuclein, causing its dispersion from the synapse. In addition to the presumed role of alpha-synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease.</div>
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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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<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>
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