The role of actomyosin contraction on actin filament stability revealed by using new easy-to-use Single-Molecule Speckle (eSiMS) microscopy.
| Project/Area Number |
15K07045
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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 |
Cell biology
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2017: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 一分子イメーシング / 定量的イメージング / メカノセンシング / アクチン / ミオシン / 一分子イメージング / 接着斑 / 細胞運動 |
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| Outline of Final Research Achievements |
How mechanical stress applied to the actin network modifies actin turnover has attracted considerable attention. Actomyosin exerts the major force on the actin network, which has been implicated in actin stability regulation. However, direct monitoring of immediate changes in F-actin stability upon alteration of actomyosin contraction has not been achieved. In this project, I reexamined myosin regulation of actin stability by using single-molecule speckle analysis of fluorescently labeled actin. I performed time-resolved analysis of the effect of blebbistatin on actin turnover. Blebbistatin enhanced actin disassembly in lamellipodia of fish keratocytes and lamellar of Xenopus XTC cells at an early stage of the inhibition, indicating that actomyosin contraction stabilizes cellular F-actin. These findings point to the power of direct viewing of molecular behavior in elucidating force regulation of actin filament turnover.
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Report
(4 results)
Research Products
(11 results)
