Oligomerization of SNARE complex by complexin
| Project/Area Number |
20700343
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | Tokushima Bunri University |
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Principal Investigator |
SHIMIZU Chigusa Tokushima Bunri University, 香川薬学部, 助教 (70435072)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2010: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2009: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2008: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
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| Keywords | シナフィン・コンプレキシン / シナプトタグミン / SNARE複合体 / コンプレキシン |
|---|
| Research Abstract |
Fast, submillisecond synaptic transmission is critical for brain function. Synaptic transmission is mediated by neurotransmitters that are exocytotically discharged by the fusion of synaptic vesicles with the presynaptic membrane. The SNARE complexe is a key step in vesicle fusion. On the other hand, synaptotagmin 1 is essential as a Ca^<2+> sensor. For Ca^<2+>-dependent exocytosis, the strong binding of SNARE complex and synaptotagmin1 is important. However, the affinity between SNARE complex and synaptotagmin1 is very low. The additional factors are needed for this interaction. One candidate for such factors includes synaphins. I reported that synaphin bound to SNARE complex in its central region and synaptotagmin 1 in C-terminal region. These results suggested that synaphin mediated the interaction between SNARE complex and synaptotagmin for Ca^<2+>-dependent exocytosis.
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Report
(4 results)
Research Products
(28 results)
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[Book] 生体の科学 612010
Author(s)
得丸博史、清水-岡部千草、阿部輝雄
Publisher
シナプス小胞の開口放出におけるシナフィンの機能.
Related Report
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