| Literature DB >> 9342384 |
V O'Connor1, C Heuss, W M De Bello, T Dresbach, M P Charlton, J H Hunt, L L Pellegrini, A Hodel, M M Burger, H Betz, G J Augustine, T Schäfer.
Abstract
The membrane protein syntaxin participates in several protein-protein interactions that have been implicated in neurotransmitter release. To probe the physiological importance of these interactions, we microinjected into the squid giant presynaptic terminal botulinum toxin C1, which cleaves syntaxin, and the H3 domain of syntaxin, which mediates binding to other proteins. Both reagents inhibited synaptic transmission yet did not affect the number or distribution of synaptic vesicles at the presynaptic active zone. Recombinant H3 domain inhibited the interactions between syntaxin and SNAP-25 that underlie the formation of stable SNARE complexes in vitro. These data support the notion that syntaxin-mediated SNARE complexes are necessary for docked synaptic vesicles to fuse.Entities:
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Year: 1997 PMID： 9342384 PMCID： PMC23745 DOI： 10.1073/pnas.94.22.12186
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205