Development of an in situ visible cell-free assay system for neurotransmitter release
Project/Area Number |
25640036
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
Neurochemistry/Neuropharmacology
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Research Institution | Kobe University |
Principal Investigator |
SAKISAKA TOSHIAKI 神戸大学, 医学(系)研究科(研究院), 教授 (80359843)
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Co-Investigator(Kenkyū-buntansha) |
YAMAMOTO YASUNORI 神戸大学, 大学院医学研究科, 准教授 (30467659)
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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Keywords | 神経伝達物質 / シナプス小胞 / 膜融合 |
Outline of Final Research Achievements |
The main process of synaptic transmission form one neuron to another neuron is mediated by neurotransmitter release. The entry of Ca2+ into nerve terminals initiates the series of molecular events that culminates with fusion of the synaptic vesicle and release of neurotransmitter into the synaptic cleft. The presynaptic membrane curvature change has been shown to be involved in the synaptic vesicle fusion. Here we identify membrane-shaping proteins, Arl6IP1 and TMCC3. We also identify an Arl6IP1-interacting protein TMEM33. TMEM33 suppresses the membrane-shaping activity of Arl6IP1. On the other hand, TMCC3 has membrane-laminating activity through interacting with membrane-shaping proteins, reticulon family proteins.
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Report
(4 results)
Research Products
(14 results)
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[Journal Article] Crystal structure of afadin PDZ domain-nectin-3 complex shows the structural plasticity of the ligand-binding site.2015
Author(s)
Fujiwara, Y., Goda, N., Tamashiro, T., Narita, H., Satomura, K., Tenno, T., Nakagawa, A., Oda, M., Suzuki, M., Sakisaka, T., Takai, Y., and Hiroaki, H.
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Journal Title
Protein Science
Volume: 24
Pages: 376-385
Related Report
Peer Reviewed
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