Robust mechanosensing and tension generation by myosin VI.

Robust mechanosensing and tension generation by myosin VI.
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DOI:
10.1016/j.jmb.2010.10.010
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发表时间:
2011-01-07
影响因子:
5.6
通讯作者:
Dunn AR
Dunn AR
中科院分区:
生物学2区
文献类型:
--
作者:
Chuan P;Spudich JA;Dunn AR

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肌球蛋白VI是一种分子马达,据认为在体内兼具转运蛋白和细胞骨架锚定蛋白的功能。在此我们利用光镊在生理核苷酸浓度下检测单个肌球蛋白VI分子产生的力。我们发现,肌球蛋白VI在负载高达约2皮牛时是一种高效的转运蛋白,但在更高负载下则作为细胞骨架锚定蛋白起作用。我们的数据以及由此产生的模型与整体结构运动和核苷酸结合及释放的间接耦合是一致的。该模型提供了一种机制,通过这种机制负载可调节肌球蛋白VI在体内的双重功能。我们的研究结果表明,肌球蛋白VI的动力学经过调整,使得该马达在细胞内维持恒定水平的机械张力,这一特性可能为其他机械敏感蛋白所共有。
Myosin VI is a molecular motor that is thought to function as both a transporter and a cytoskeletal anchor in vivo. Here we use optical tweezers to examine force generation by single molecules of myosin VI under physiological nucleotide concentrations. We find that myosin VI is an efficient transporter at loads up to ~2 pN but acts as a cytoskeletal anchor at higher loads. Our data and resulting model are consistent with an indirect coupling of global structural motions to nucleotide binding and release. The model provides a mechanism by which load may regulate the dual functions of myosin VI in vivo. Our results suggest that myosin VI kinetics are tuned such that the motor maintains a consistent level of mechanical tension within the cell, a property potentially shared by other mechanosensitive proteins.
肌球蛋白我可以充当分子力传感器。
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