Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses Journal Article


Authors: Schiavo, G.; Stenbeck, G.; Rothman, J. E.; Söllner, T. H.
Article Title: Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses
Abstract: Neurotransmitter release requires the specific docking of synaptic vesicles to the presynaptic plasma membrane followed by a calcium-triggered fusion event. Herein we report a previously unsuspected interaction of the synaptic vesicle protein and likely calcium sensor synaptotagmin with the plasma membrane t-SNARE SNAP-25. This interaction appears to resolve the apparent paradox that synaptic vesicles are capable of docking even when VAMP (vesicle-associated membrane protein) or syntaxin is cleaved or deleted and suggests that two species of v-SNAREs (VAMP and synaptotagmin) and two species of t-SNAREs (SNAP-25 and syntaxin) interact to functionally dock synaptic vesicles.
Keywords: animals; nerve tissue proteins; membrane proteins; calcium; recombinant fusion proteins; membrane glycoproteins; presynaptic terminals; cell membrane; cattle; calcium-binding proteins; cerebral cortex; synaptotagmin; membrane binding; exocytosis; fusion; vesicular transport proteins; calcium transport; neurotransmission; synaptic transmission; membrane fusion; botulinum toxins; neurotransmitter release; syntaxin; docking protein; neurotransmitter; qa-snare proteins; r-snare proteins; snare proteins; synaptic vesicles; synapse vesicle; synaptosomal-associated protein 25; synaptobrevin; priority journal; article; synaptotagmins; neurotoxin
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 94
Issue: 3
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1997-02-04
Start Page: 997
End Page: 1001
Language: English
DOI: 10.1073/pnas.94.3.997
PUBMED: 9023371
PROVIDER: scopus
PMCID: PMC19628
DOI/URL:
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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  1. Thomas H Sollner
    65 Sollner
  2. James E Rothman
    120 Rothman