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| A PROTEIN ASSEMBLY-DISASSEMBLY PATHWAY IN-VITRO THAT MAY CORRESPOND TO SEQUENTIAL STEPS OF SYNAPTIC VESICLE DOCKING, ACTIVATION, AND FUSION |
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| Author(s): SOLLNER T, BENNETT MK, WHITEHEART SW, SCHELLER RH, ROTHMAN JE |
| Source: CELL Volume: 75 Issue: 3 Pages: 409-418 Published: NOV 5 1993 |
| Times Cited: 1,165 References: 55 |
| 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 alpha-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 alpha-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. |
| Document Type: Article |
| Language: English |
| Reprint Address: SOLLNER, T (reprint author), MEM SLOAN KETTERING CANC CTR, PROGRAM CELLULAR BIOCHEM & BIOPHYS, NEW YORK, NY 10021 USA |
Addresses:
1. STANFORD UNIV, MED CTR, HOWARD HUGHES MED INST, DEPT MOLEC & CELLULAR PHYSIOL, STANFORD, CA 94305 USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: MF830 |
| ISSN: 0092-8674 |
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