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Vol. 13, Issue 8, 2706-2717, August 2002

Fluorescence Resonance Energy Transfer Detection of Synaptophysin I and Vesicle-associated Membrane Protein 2 Interactions during Exocytosis from Single Live Synapses

Maria Pennuto,^* David Dunlap,^* Andrea Contestabile,^* Fabio Benfenati, and Flavia Valtorta^*

 ^*Department of Neuroscience, S. Raffaele Scientific Institute and "Vita-Salute" University, Milan, Italy; and  Department of Experimental Medicine, Section of Human Physiology, University of Genoa, Italy

To investigate the molecular interactions of synaptophysin I and vesicle-associated membrane protein 2 (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 soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex and possibly participating in the late steps of exocytosis.

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Corresponding author. E-mail address: valtorta.flavia{at}hsr.it.

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Molecular Biology of the Cell
Vol. 13, 2706-2717, August 2002
Copyright © 2002 by The American Society for Cell Biology

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