Nano-mechanical Behaviors of Tension-sensoring Proteins
| Project/Area Number |
15K13832
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Materials/Mechanics of materials
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| Research Institution | Kyoto University |
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Principal Investigator |
Adachi Taiji 京都大学, ウイルス・再生医科学研究所, 教授 (40243323)
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| Co-Investigator(Kenkyū-buntansha) |
井上 康博 京都大学, ウイルス・再生医科学研究所, 准教授 (80442929)
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 張力感受センサー分子 / ナノ構造力学試験 / 原子間力顕微鏡 / ナノバイオメカニクス / αカテニン / ナノ力学試験 / ナノフィッシング / 分子動力学解析 |
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| Outline of Final Research Achievements |
At adherens junctions, α-catenin is known to act as a tension sensor and accelerate the positive feedback of intercellular tension by recruiting vinculin. In this study, we aimed at elucidating the mechanism how α-catenin retains its activated state while avoiding unfolding under tension. Based on nano-tensile testing using atomic force microscopy, we found that mechanically activated α-catenin fragment exhibited higher mechanical stability than a non-activated one. Through the comparison with mutated and segmented fragments, we found that the key intramolecular interactions within α-catenin act as a conformational switch. We also demonstrated that α-catenin adaptively changes its conformation under tension to a stable intermediate state and settles into a more stable state reinforced by vinculin binding. Our findings suggest that the characteristics of α-catenin enable the functional dynamics of multicellular tissues.
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Report
(3 results)
Research Products
(11 results)
