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First published online 20 May 2003
doi: 10.1242/jcs.00467
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Research Article |
1 Membrane Traffic and Neuronal Plasticity, INSERM U536, Institut du
Fer-à-Moulin, 75005 Paris, France
2 Morphogenesis and Cell Signaling, CNRS UMR 144, Institut Curie, 75005 Paris,
France
* Author for correspondence (e-mail: galli{at}idf.inserm.fr)
Accepted 10 March 2003
SNARE proteins are key mediators of membrane fusion. Their function in ensuring compartmental specificity of membrane fusion has been suggested by in vitro studies but not demonstrated in vivo. We show here that ectopic expression of the plasma membrane t-SNARE heavy chain syntaxin 1 in the endoplasmic reticulum induces the redistribution of its cognate vesicular SNAREs, TI-VAMP and cellubrevin, and its light chain t-SNARE SNAP-23. These effects were prevented by co-expressing nSec1. Expression of syntaxin 1 alone impaired the cell surface expression of TI-VAMP and cellubrevin but not the recycling of transferrin receptor. TI-VAMP, cellubrevin and SNAP-23 associated in vivo with exogenous syntaxin 1. Redistribution of TI-VAMP in the ER of syntaxin-1-expressing cells was microtubule dependent and impaired the trafficking of CD63, a cargo of TI-VAMP-containing vesicles. We conclude that the destination of v-SNAREs is driven by their specific interaction with cognate t-SNAREs. Our in vivo data provide strong support for the theory that highly specific v-SNARE–t-SNARE interactions control compartmental specificity of membrane fusion.
Key words: Membrane fusion, SNARE proteins, TI-VAMP, Cellubrevin, Syntaxin
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