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A more recent version of this article appeared on December 1, 2003
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Submitted on June 10, 2003
Revised on July 24, 2003
Accepted on July 30, 2003
1 Dept. of Neuroscience, S. Raffaele Scientific Institute and "Vita-Salute" University, Milano, Italy
2 Dept. of Experimental Medicine, Section of Human Physiology, University of Genova, Italy
* Corresponding author. E-mail address: valtorta.flavia{at}hsr.it.
Synaptic vesicle (SV) proteins are synthesized at the level of the cell body and transported down the axon in membrane precursors of SVs. To investigate the mechanisms underlying sorting of proteins to SVs, fluorescent chimeras of vesicle-associated membrane protein (VAMP) 2, its highly homologous isoform VAMP1 and synaptotagmin I (SytI) were expressed in hippocampal neurons in culture. Interestingly, the proteins displayed a diffuse component of distribution along the axon. In addition, VAMP2 was found to travel in vesicles which constitutively fuse with the plasma membrane. Coexpression of VAMP2 with synaptophysin I (SypI), a major resident of SVs, restored the correct sorting of VAMP2 to SVs. The effect of SypI on VAMP2 sorting was dose-dependent, being reversed by increasing VAMP2 expression levels, and highly specific, since the sorting of the SV proteins VAMP1 and SytI was not affected by SypI. The cytoplasmic domain of VAMP2 was found to be necessary for both the formation of VAMP2-SypI hetero-dimers and for VAMP2 sorting to SVs. These data support a role for SypI in directing the correct sorting of VAMP2 in neurons, and demonstrate that a direct interaction between the two proteins is required for SypI in order to exert its effect.
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