2011 Fiscal Year Final Research Report
Structural polymorphism and functional differentiation of actin filaments
| Project/Area Number |
21370061
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | National Institute of Advanced Industrial Science and Technology |
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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, 部門付 (90356551)
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| Co-Investigator(Kenkyū-buntansha) |
TOKURAKU Kiyotaka 室蘭工業大学, 大学院・工学研究科, 准教授 (00332106)
KATAYAMA Eisaku 千葉大学, 大学院・工学研究科, 研究員 (50111505)
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| Project Period (FY) |
2009 – 2011
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| Keywords | アクチンフィラメント / ミオシン / コフィリン / 協同的結合 / 張力 / メカノセンサー / 細胞極性 |
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| Research Abstract |
The goal of this project is to understood how different actin filaments within a cell perform different functions. We found that stretched actin filaments with a longer helical pitch have higher affinity for myosin II. We also found that myosin II and cofilin, two major actin binding proteins, bound to actin filaments in a mutually exclusive manner, even though the two proteins do not compete for a binding site on actin. These results support our hypothesis that actin filaments of different atomic structures have different affinities for different actin binding proteins, leading to functional differentiation within cells.
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[Journal Article] G146V mutation at the hinge region of actin reveals a myosin class-specific requirement of actin conformations for motility2012
Author(s)
Noguchi, T. Q. P., T. Komori, N. Umeki N. Demizu, K. Ito, A. Hikikoshi-Iwane, K. Tokuraku, T. Yanagida and T. Q. P.Noguchi, T. Q. P., T. Komori, N. Umeki N. Demizu, K. Ito, A. Hikikoshi-Iwane, K. Tokuraku, T. Yanagida and T. Q. P. Uyeda
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Journal Title
J. Biol. Chem.
Volume: (in press)
URL
Peer Reviewed
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