Timing of synaphin action in neurotransmitter release
Project/Area Number |
17590082
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biological pharmacy
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Research Institution | Tokushima Bunri University |
Principal Investigator |
TOKUMURA Hiroshi Tokushima Bunri University, Pharmaceutical Science at Kagawa, Associate Professor, 香川薬学部, 助教授 (70262160)
|
Co-Investigator(Kenkyū-buntansha) |
ABE Teruo Niigata University, Brain Research Institute, Associate Professor, 脳研究所, 助教授 (50010103)
YAMAGUCHI Kentaro Tokushima Bunri University, Pharmaceutical Science at Kagawa, Professor, 香川薬学部, 教授 (50159208)
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Project Period (FY) |
2005 – 2006
|
Project Status |
Completed (Fiscal Year 2006)
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Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2006: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2005: ¥2,200,000 (Direct Cost: ¥2,200,000)
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Keywords | syntaxin / synaptic transmission / caged peptide / neurotransmitter release / SNARE complex / スネアー複合体 |
Research Abstract |
The exocytotic release of neurotransmitters at synapses requires the temporally-ordered trafficking of synaptic vesicles. More than 20 proteins are involved in this process^<1-3>, including the SNARE proteins that participate in membrane fusion during exocytosis^<4,5>. To discern the specific role that each protein plays, it is necessary to sort out the temporal order in which they interact. Here we pinpoint the time of action of synaphin/complexin, a protein that participates in neurotransmitter release by binding to SNAREs. A synthetic, light-activated inhibitory peptide was designed to block the binding of synaphin to SNARE proteins at precise times. We find that this peptide inhibits neurotransmitter release within 180 milliseconds before fusion of synaptic vesicles with the presynaptic plasma membrane, preventing these vesicles from participating in the readily releasable pool. These results indicate that synaphin binds to the SNARE complex soon after synaptic vesicles dock, but well before the millisecond required for calcium ions to trigger synaptic vesicle fusion. These observations indicate that synaphin prepares SNARE complexes for membrane fusion and document an experimental approach that can be used to define the temporal order of the many other protein-protein interactions underlying neurotransmitter release.
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Report
(3 results)
Research Products
(2 results)