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- Title
Neural Activity Controls the Synaptic Accumulation of α-Synuclein.
- Authors
Fortin, Doris L.; Nemani, Venu M.; Voglmaier, Susan M.; Anthony, Malcolm D.; Ryan, Timothy A.; Edwards, Robert H.
- Abstract
The presynaptic protein α-synuclein has a central role in Parkinson's disease (PD). However, the mechanism by which the protein contributes to neurodegeneration and its normal function remain unknown. α-Synuclein localizes to the nerve terminal and interacts with artificial membranes in vitro but binds weakly to native brain membranes. To characterize the membrane association of α-synuclein in living neurons, we used fluorescence recovery after photobleaching. Despite its enrichment at the synapse, α-synuclein is highly mobile, with rapid exchange between adjacent synapses. In addition, we find that α-synuclein disperses from the nerve terminal in response to neural activity. Dispersion depends on exocytosis, but unlike other synaptic vesicle proteins, α-synuclein dissociates from the synaptic vesicle membrane after fusion. Furthermore, the dispersion of α-synuclein is graded with respect to stimulus intensity. Neural activity thus controls the normal function of α-synuclein at the nerve terminal and may influence its role in PD.
- Subjects
PROTEINS; PARKINSON'S disease; NEURONS; FLUORESCENCE; SYNAPSES
- Publication
Journal of Neuroscience, 2005, Vol 25, Issue 47, p10913
- ISSN
0270-6474
- Publication type
Article
- DOI
10.1523/JNEUROSCI.2922-05.2005