| Project/Area Number |
17K07309
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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 |
Structural biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
Shimada Atsushi 九州大学, 生体防御医学研究所, 准教授 (70391977)
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| Project Period (FY) |
2017-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2019: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2018: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 蛋白質 / X線結晶構造解析 / 等温滴定熱測定 / エンドサイトーシス / 蛋白質間相互作用 / 電子顕微鏡 / X線結晶解析 / タンパク質間相互作用 |
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| Outline of Final Research Achievements |
Clathrin-mediated endocytosis is a mechanism by which eukaryotic cells take up extracellular molecules into the cell. Clathrin-mediated endocytosis is initiated by a process called clathrin assembly, where a pivotal protein, clathrin, assembles into the clathrin lattice on the cell membrane. Among the proteins responsible for clathrin assembly, some proteins localize to the central part of the lattice and others localize to the periphery of the lattice, thereby forming a complex network to promote clathrin assembly. In this study, we used structural biological and biochemical techniques and elucidated the structural basis for the interactions of the key molecules of clathrin assembly, such as Eps15 and the AP-2 complex. Based on these results, we constructed a novel mechanistic model of clathrin assembly.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究ではクラスリン依存性エンドサイトーシスのクラスリン重合ステップに関与するタンパク質について、その相互作用の構造的基盤を解明し、新たなクラスリン重合モデルを構築した。この成果は真核生物における普遍的な生命現象であるクラスリン依存性エンドサイトーシス進行機構の理解を深めるだけでなく、近年注目を集める、クラスリン依存性エンドサイトーシスをターゲットにした創薬の基礎にもなる成果である。
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