当前位置: X-MOL 学术Sci. Adv. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Different motilities of microtubules driven by kinesin-1 and kinesin-14 motors patterned on nanopillars.
Science Advances ( IF 13.6 ) Pub Date : 2020-01-22 , DOI: 10.1126/sciadv.aax7413
Taikopaul Kaneko 1 , Ken'ya Furuta 2 , Kazuhiro Oiwa 2 , Hirofumi Shintaku 1, 3 , Hidetoshi Kotera 1, 4 , Ryuji Yokokawa 1
Affiliation  

Kinesin is a motor protein that plays important roles in a variety of cellular functions. In vivo, multiple kinesin molecules are bound to cargo and work as a team to produce larger forces or higher speeds than a single kinesin. However, the coordination of kinesins remains poorly understood because of the experimental difficulty in controlling the number and arrangement of kinesins, which are considered to affect their coordination. Here, we report that both the number and spacing significantly influence the velocity of microtubules driven by nonprocessive kinesin-14 (Ncd), whereas neither the number nor the spacing changes the velocity in the case of highly processive kinesin-1. This result was realized by the optimum nanopatterning method of kinesins that enables immobilization of a single kinesin on a nanopillar. Our proposed method enables us to study the individual effects of the number and spacing of motors on the collective dynamics of multiple motors.

中文翻译:

kinesin-1和kinesin-14电机驱动的微管在纳米柱上的模式不同。

驱动蛋白是一种运动蛋白,在多种细胞功能中起重要作用。在体内,多个驱动蛋白分子与货物结合,并作为一个团队共同产生比单个驱动蛋白更大的力或更高的速度。但是,由于实验上难以控制驱动蛋白的数量和排列,因此对驱动蛋白的协调性仍然知之甚少,这被认为会影响它们的协调性。在这里,我们报告数量和间隔都显着影响非持续性驱动蛋白14(Ncd)驱动的微管的速度,而在高度持续性驱动蛋白1的情况下,数量和间隔都不会改变速度。该结果是通过最佳的驱动蛋白纳米图案方法实现的,该方法能够将单个驱动蛋白固定在纳米柱上。
更新日期:2020-01-23
down
wechat
bug