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A more recent version of this article appeared on August 1, 2002
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Submitted on January 22, 2002
Revised on March 28, 2002
Accepted on May 7, 2002
1 Department Neuroscience, S. Raffaele Scientific Institute and "Vita-Salute" University, Milan, Italy
2 Department Experimental Medicine, Section of Human Physiology, University of Genoa, Italy
* Corresponding author. E-mail address: valtorta.flavia{at}hsr.it.
To investigate the molecular interactions of synaptophysin I and VAMP2/synaptobrevin II during exocytosis, we have used time-lapse videomicroscopy to measure fluorescence resonance energy transfer in live neurons. For this purpose, fluorescent protein variants fused to synaptophysin I or VAMP2 were expressed in rat hippocampal neurons. We show that synaptophysin I and VAMP2 form both homo- and hetero-oligomers on the synaptic vesicle membrane. When exocytosis is stimulated with 
-latrotoxin, VAMP2 dissociates from synaptophysin I even in the absence of appreciable exocytosis, whereas synaptophysin I oligomers disassemble only upon incorporation of the vesicle with the plasma membrane. We propose that synaptophysin I has multiple roles in neurotransmitter release, regulating VAMP2 availability for the SNARE complex and possibly participating in the late steps of exocytosis.
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