| Project/Area Number |
15K07384
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
Shibata Hideki 名古屋大学, 生命農学研究科, 准教授 (30314470)
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| Co-Investigator(Renkei-kenkyūsha) |
MAKI Masatoshi 名古屋大学, 大学院生命農学研究科, 教授 (40183610)
TAKAHARA Terunao 名古屋大学, 大学院生命農学研究科, 助教 (90708059)
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| Research Collaborator |
KUWATA Keiko 名古屋大学, トランスフォーマティブ生命分子研究所, 特任助教 (70624352)
KANADOME Takashi 名古屋大学, 大学院生命農学研究科, 大学院生
SATO Akane 名古屋大学, 大学院生命農学研究科, 大学院生
INOUE Kuniko 名古屋大学, 大学院生命農学研究科, 大学院生
ARAI Yumika 名古屋大学, 大学院生命農学研究科, 大学院生
KONO Yuta 名古屋大学, 大学院生命農学研究科, 大学院生
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2015: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | カルシウム / COPII小胞 / 分泌経路 / タンパク質間相互作用 / 小胞体 / 小胞輸送 |
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| Outline of Final Research Achievements |
In mammalian cells, proteins destined for secretion are transported from specialized region of the ER, called ER exit site (ERES), by COPII vesicles. The aim of this study was to investigate the role of ALG-2, a calcium-binding protein, in the regulation of COPII-mediated protein transport. ALG-2 directly interacts with Sec31A, an outer coat component of COPII. Firstly, we identified Trk-fused gene (TFG) product as a novel target for ALG-2. Overexpression of ALG-2 enhanced the localization of TFG to the ERES. Secondly, MISSL was shown to be recruited to the ERES by ALG-2 in response to calcium mobilization. We also found that ALG-2 bridged between MISSL and MAP1B. In our co-immunoprecipitation analysis, TFG, MISSL and MAP1B did not form the complex with Sec31A, suggesting that ALG-2 may have divergent functions at the ERES. Finally, we reported that amyotrophic lateral sclerosis (ALS)-associated mutations in annexin A11 caused abnonormality in binding to S100A6.
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