A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion Journal Article
| Authors: | Söllner, T.; Bennett, M. K.; Whiteheart, S. W.; Scheller, R. H.; Rothman, J. E. |
| Article Title: | A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion |
| Abstract: | The SNARE hypothesis holds that a transport vesicle chooses its target for fusion when a soluble NSF attachment protein (SNAP) receptor on the vesicle (v-SNARE) pairs with its cognate t-SNARE at the target membrane. Three synaptosomal membrane proteins have previously been identified: syntaxin, SNAP-25 (t-SNAREs), and vesicle-associated membrane protein (VAMP) (v-SNARE); all assemble with SNAPs and NSF into 20S fusion particles. We now report that in the absence of SNAP and NSF, these three SNAREs form a stable complex that can also bind synaptotagmin. Synaptotagmin is displaced by α-SNAP, suggesting that these two proteins share binding sites on the SNARE complex and implying that synaptotagmin operates as a "clamp" to prevent fusion from proceeding in the absence of a signal. The α-SNAP-SNARE complex can bind NSF, and NSF-dependent hydrolysis of ATP dissociates the complex, separating syntaxin, SNAP-25, and VAMP. ATP hydrolysis by NSF may provide motion to initiate bilayer fusion. © 1993. |
| Keywords: | animal; models, biological; protein assembly; nerve tissue proteins; protein binding; fluorescent antibody technique; hybrid protein; brain; membrane glycoproteins; carrier proteins; membrane protein; cattle; adenosine triphosphate; signal processing; hydrolysis; receptor binding; bilayer membrane; antigens, surface; polyacrylamide gel electrophoresis; exocytosis; membrane fusion; pc12 cells; synaptic vesicles; synapse vesicle; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; adenosinetriphosphatase |
| Journal Title: | Cell |
| Volume: | 75 |
| Issue: | 3 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1993-11-05 |
| Start Page: | 409 |
| End Page: | 418 |
| Language: | English |
| DOI: | 10.1016/0092-8674(93)90376-2 |
| PUBMED: | 8221884 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Source: Scopus |
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