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Neural Activity Controls the Synaptic Accumulation of α-Synuclein
Doris L. Fortin (University of California, San Francisco), Venu M. Nemani (University of California, San Francisco), Susan M. Voglmaier (University of California, San Francisco), Malcolm D. Anthony (University of California, San Francisco), Timothy A. Ryan (Cornell University, Weill Cornell Medicine), Robert H. Edwards (University of California, San Francisco)
Résumé : The presynaptic protein alpha-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. Alpha-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 alpha-synuclein in living neurons, we used fluorescence recovery after photobleaching. Despite its enrichment at the synapse, alpha-synuclein is highly mobile, with rapid exchange between adjacent synapses. In addition, we find that alpha-synuclein disperses from the nerve terminal in response to neural activity. Dispersion depends on exocytosis, but unlike other synaptic vesicle proteins, alpha-synuclein dissociates from the synaptic vesicle membrane after fusion. Furthermore, the dispersion of alpha-synuclein is graded with respect to stimulus intensity. Neural activity thus controls the normal function of alpha-synuclein at the nerve terminal and may influence its role in PD.