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dc.contributor.authorYu, Szi-Chieh
dc.contributor.authorKlosterman, Susan M.
dc.contributor.authorMartin, Ashley A.
dc.contributor.authorRichmond, Janet E.
dc.date.accessioned2013-12-03T21:53:56Z
dc.date.available2013-12-03T21:53:56Z
dc.date.issued2013-02
dc.identifier.bibliographicCitationYu SC, Klosterman SM, Martin AA, Gracheva EO, Richmond JE. Differential roles for snapin and synaptotagmin in the synaptic vesicle cycle. PLoS One. 2013;8(2):e57842. doi: 10.1371/journal.pone.0057842.en_US
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/10027/10761
dc.description© 2013 Yu et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. © 2013 by Public Library of Science, PLoS ONE.en_US
dc.description.abstractEvoked synaptic transmission is dependent on interactions between the calcium sensor Synaptotagmin I and the SNARE complex, comprised of Syntaxin, SNAP-25, and Synaptobrevin. Recent evidence suggests that Snapin may be an important intermediate in this process, through simultaneous interactions of Snapin dimers with SNAP-25 and Synaptotagmin. In support of this model, cultured neurons derived from embryonically lethal Snapin null mutant mice exhibit desynchronized release and a reduced readily releasable vesicle pool. Based on evidence that a dimerization-defective Snapin mutation specifically disrupts priming, Snapin is hypothesized to stabilize primed vesicles by structurally coupling Synaptotagmin and SNAP-25. To explore this model in vivo we examined synaptic transmission in viable, adult C. elegans Snapin (snpn-1) mutants. The kinetics of synaptic transmission were unaffected at snpn-1 mutant neuromuscular junctions (NMJs), but the number of docked, fusion competent vesicles was significantly reduced. However, analyses of snt-1 and snt-1;snpn-1 double mutants suggest that the docking role of SNPN-1 is independent of Synaptotagmin. Based on these results we propose that the primary role of Snapin in C. elegans is to promote vesicle priming, consistent with the stabilization of SNARE complex formation through established interactions with SNAP-25 upstream of the actions of Synaptotagmin in calcium-sensing and endocytosis.en_US
dc.description.sponsorshipThis study was funded by NIH R01 MH073156-03.en_US
dc.language.isoen_USen_US
dc.publisherPublic Library of Scienceen_US
dc.titleDifferential Roles for Snapin and Synaptotagmin in the Synaptic Vesicle Cycleen_US
dc.typeArticleen_US


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