Structural changes in the actin filament associated with tension sensing
| Project/Area Number |
23612003
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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 |
Mechanobiology
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| Research Institution | Nagoya University |
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Principal Investigator |
TATSUMI Hitoshi 名古屋大学, 医学(系)研究科(研究院), 准教授 (20171720)
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| Co-Investigator(Kenkyū-buntansha) |
HAYAKAWA Kimihide 名古屋大学, 大学院医学系研究科, 特任講師 (60467280)
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| Co-Investigator(Renkei-kenkyūsha) |
SOKABE Masahiro 名古屋大学, 大学院医学系研究科, 特任教授 (10093428)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | アクチン / コフィリン / 力学刺激 / 切断 / 光ピンセット / 一分子イメージング / 分子ゆらぎ / 近接場光 / アクチン線維 / 力受容 / イメージング / 一分子操作 / 分子ねじれ / ゆらぎ / mechanosensor / cofilin / actin |
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| Research Abstract |
Molecular and biophysical mechanisms, including how mechanical forces are sensed, are totally unknown. ADF/cofilin proteins are the most preferable candidate for the stress fiber disassembly induced by tension decline in the fiber. Here, we propose a hypothesis that tension in an actin filament prevents the filament from being severed by cofilin. To test this, we prepared single actin filaments tensed with optical tweezers. When the fiber was tensed, it was severed after the application of cofilin with a significantly larger delay in comparison with the control filaments. Direct measurement of the torsional fluctuation of a single actin filament was made under different stresses, which indicated that the standard deviation of the fluctuation was reduced by an applied force of ca. 5 pN. These results demonstrate that tension in the actin filament reduces the binding of cofilin, resulting in a decrease in the effective severing activity of cofilin.
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Report
(4 results)
Research Products
(24 results)
