| Project Area | Harmonized supramolecular machinery for motility and its diversity |
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| Project/Area Number |
24117008
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| Research Category |
Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | Waseda University (2016)
National Institute of Advanced Industrial Science and Technology (2012-2015) |
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Principal Investigator |
Uyeda Taro 早稲田大学, 理工学術院, 教授 (90356551)
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| Co-Investigator(Kenkyū-buntansha) |
徳樂 清孝 室蘭工業大学, 工学(系)研究科(研究院), 准教授 (00332106)
長崎 晃 国立研究開発法人産業技術総合研究所, バイオメディカル研究部門, 主任研究員 (30392640)
野口 太郎 都城工業高等専門学校, 物質工学科, 講師 (90615866)
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| Co-Investigator(Renkei-kenkyūsha) |
KATAYAMA Eisaku 大阪市立大学, 理学部, 特任教授 (50111505)
WAKABAYASHI Takeyuki 帝京大学, 理工学部, 教授 (90011717)
TAKANO Mitsunori 早稲田大学, 理工学術院, 教授 (40313168)
GOMIBUCHI Yuki 帝京大学, 理工学部, 博士研究員 (10740219)
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| Research Collaborator |
Ngo Xuan Kien
SHIBATA Keitaro
ADACHI Kengo
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| Project Period (FY) |
2012-06-28 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥87,100,000 (Direct Cost: ¥67,000,000、Indirect Cost: ¥20,100,000)
Fiscal Year 2016: ¥17,810,000 (Direct Cost: ¥13,700,000、Indirect Cost: ¥4,110,000)
Fiscal Year 2015: ¥17,810,000 (Direct Cost: ¥13,700,000、Indirect Cost: ¥4,110,000)
Fiscal Year 2014: ¥17,810,000 (Direct Cost: ¥13,700,000、Indirect Cost: ¥4,110,000)
Fiscal Year 2013: ¥17,680,000 (Direct Cost: ¥13,600,000、Indirect Cost: ¥4,080,000)
Fiscal Year 2012: ¥15,990,000 (Direct Cost: ¥12,300,000、Indirect Cost: ¥3,690,000)
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| Keywords | アクチン / ミオシン / コフィリン / 構造多型性 / アロステリー / 細胞運動 / FRET / 高速原子間力顕微鏡 / 高速AFM / 協同的構造変化 / 協同性 / アクチン結合タンパク質 / 全反射顕微鏡 / 全反射蛍光顕微鏡 / 構造多型 / 蛍光顕微鏡 / メカノセンサー |
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| Outline of Final Research Achievements |
(1) It had been shown that cofilin binds cooperatively to actin filaments (AFs) forming clusters, and that the helix of AF in the cluster is supertwisted. We demonstrated that the conformational changes in AF are propagated to the neighboring bare zone on the pointed end side of the cluster, which leads to unidirectional growth of cofilin clusters along AFs. (2) In contrast, we found that transient interactions of AFs with S1 in the presence of ATP induce a different, untwisting conformational changes to AFs, which strongly inhibit cofilin binding. Thus, we showed that the two actin binding proteins (ABPs) induce different cooperative conformational changes to AFs, leading to enhancement or inhibition of ABP binding. Based on the results of those in vitro experiments, we proposed that cooperative conformational changes of AFs play major roles in specifying the functions of AF in vivo. (3) Consistent with this hypothesis, we demonstrated that AFs in cells are polymorphic.
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