Journal
STRUCTURE
Volume 16, Issue 2, Pages 308-320Publisher
CELL PRESS
DOI: 10.1016/j.str.2007.12.010
Keywords
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIMH NIH HHS [R01 MH063105, MH63105, R01 MH081923, R01 MH081923-01, R37 MH063105, R01 MH063105-09] Funding Source: Medline
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Syntaxin/SNAP-25 interactions precede assembly of the ternary SNARE complex that is essential for neurotransmitter release. This binary complex has been difficult to characterize by bulk methods because of the prevalence of a 2:1 dead-end species. Here, using single-molecule fluorescence, we find the structure of the 1:1 syntaxin/SNAP-25 binary complex is variable, with states changing on the second timescale. One state corresponds to a parallel three-helix bundle, whereas other states show one of the SNAP-25 SNARE domains dissociated. Adding synaptobrevin suppresses the dissociated helix states. Remarkably, upon addition of complexin, Munc13, Munc18, or synaptotagmin, a similar effect is observed. Thus, the 1:1 binary complex is a dynamic acceptor for synaptobrevin binding, and accessory proteins stabilize this acceptor. In the cellular environment the binary complex is actively maintained in a configuration where it can rapidly interact with synaptobrevin, so formation is not likely a limiting step for neurotransmitter release.
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