Tension-induced conformational changes of actin filaments and their influence on actin binding and intracellular localization of myosin.
Project/Area Number |
24370069
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | National Institute of Advanced Industrial Science and Technology |
Principal Investigator |
UYEDA Taro 独立行政法人産業技術総合研究所, バイオメディカル研究部門, 総括研究主幹 (90356551)
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Co-Investigator(Kenkyū-buntansha) |
YUMURA Shigehiko 山口大学, 医学研究科, 教授 (70183986)
HAGA Hisashi 北海道大学, 先端生命科学研究科, 教授 (00292045)
NOGUCHI Taro 都城工業高等専門学校, 物質工学科, 講師 (90615866)
|
Research Collaborator |
ADACHI Taiji 京都大学, 再生医科学研究所, 教授 (40243323)
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Project Period (FY) |
2012-04-01 – 2015-03-31
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Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥17,940,000 (Direct Cost: ¥13,800,000、Indirect Cost: ¥4,140,000)
Fiscal Year 2014: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
Fiscal Year 2013: ¥7,280,000 (Direct Cost: ¥5,600,000、Indirect Cost: ¥1,680,000)
Fiscal Year 2012: ¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
|
Keywords | アクチン / ミオシン / メカノセンシティビティ / メカノセンサー / 構造多型性 / 細胞運動 / 細胞極性 / MDシミュレーション / 蛍光プローブ |
Outline of Final Research Achievements |
To elucidate the mechanism by which actin filaments perform different functions in vivo, we tested the hypothesis that tension applied to actin filaments increases affinity for myosin II. We were able to estimate the tension applied to actin filaments in amoeba cells. Experimental system to visualize myosin binding to tensed actin filaments in vitro was established, opening an avenue to directly test the hypothesis in vitro in the future. Some progress was also made in attempts to visualize tensed actin filaments in amoeba cells using a FRET-based system, demonstrating that the actin filaments in cells are polymorphic.
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Report
(4 results)
Research Products
(62 results)
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[Journal Article] Coating extracelular matrix proteins on a (3-aminopropyl)triethoxysilane-treated glass substrate for improved cell culture.2014
Author(s)
Masuda, H.T., Ishihara, S., Harada, I., Mizutani, T., Ishikawa, M., Kawabata, K., Haga, H..
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Journal Title
Biotechniques
Volume: 56
Issue: 4
Pages: 172-179
DOI
Related Report
Peer Reviewed
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[Journal Article] ADF/cofilin is not essential but is crucially important for actin activities during phagocytosis in Tetrahymena thermophila.2013
Author(s)
Shiozaki, N., Nakano, K., Kushida, Y., Noguchi, T.Q.P., Uyeda, T.Q.P., Wloga, D., Dave, D., Vasudevan, K. K., Gaertig, J., Numata, O.
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Journal Title
Eukaryotic Cell
Volume: 12
Issue: 8
Pages: 1080-1086
DOI
Related Report
Peer Reviewed
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[Journal Article] Cell-scale dynamic recycling arid cortical flow of the actin-myosin cytoskeleton for rapid cell migration2013
Author(s)
Yumura, S., Itoh, G., Kikuta, Y., Kikuchi, T., Kitanishi-Yumura, T. and Tsujioka, M.
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Journal Title
Biol. Open
Volume: 2
Issue: 2
Pages: 200-209
DOI
Related Report
Peer Reviewed
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[Journal Article] G146V mutation at the hinge region of actin reveals a myosin class-specific requirement of actin conformations for motility.2012
Author(s)
Noguchi, T. Q. P., Komori, T., Umeki, N., Demizu, N., Ito, K., Iwane, A. H., Tokuraku, K., Yanagida, T., Uyeda, T. Q. P.
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Journal Title
J. Biol. Chem.
Volume: 279
Issue: 29
Pages: 24399-34345
DOI
Related Report
Peer Reviewed
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[Journal Article] Rapid nucleotide exchange renders Asp-11 mutant actins resistant to depolymerizing activity of cofilin, leading to dominant toxicity in vivo.2012
Author(s)
Umeki, N., Nakajima, J., Noguchi, T.Q.P., Tokuraku, K., Nagasaki, A., Ito, K., Hirose, K. and Uyeda, T.Q.P.
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Journal Title
J. Biol. Chem.
Volume: 288
Issue: 3
Pages: 1739-1748
DOI
Related Report
Peer Reviewed
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[Journal Article] Talin couples the actomyosin cortex to the plasma membrane during rear retraction and cytokinesis.2012
Author(s)
Tsujioka, M., Yumura, S., Inouye, K., Patel, H., Ueda, M. and Yonemura, S.
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Journal Title
Proc. Natl. Acad. Sci. USA.
Volume: 109
Issue: 32
Pages: 12992-12997
DOI
Related Report
Peer Reviewed
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