Kinesin-4 motor proteins at nanomolar concentrations can accumulate at microtubule plus ends, regulating the microtubule length. Recent experimental studies showed that at picomolar motor concentrations, under which nearly no motor crowding can occur, the run length of the kinesin-4 motor increases whereas the velocity decreases with the motor concentration, indicating the presence of a long-range communication between the motors through the microtubule track. However, the mechanism of the long-range communication is illusive. Here, based on the proposal that large conformational changes of the tubulin induced by the strong interaction with a kinesin head can propagate along the microtubule such that influence the tubulin-binding energy of other motors distant away, the dynamics of the kinesin-4 motor at the picomolar motor concentrations is studied theoretically, explaining quantitatively the experimental data. Moreover, the lifetime of the motor when multiple motors are jammed near the plus ends at high motor concentrations is studied theoretically.

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通过微管轨道进行通信的驱动蛋白 4 马达协作模型

纳摩尔浓度的驱动蛋白 4 运动蛋白可以在微管正端积聚，调节微管长度。最近的实验研究表明，在皮摩尔运动浓度下，几乎不会发生运动拥挤，kinesin-4 运动的运行长度增加，而速度随着运动浓度的增加而减小，这表明运动之间存在长距离通信通过微管轨道。然而，远程通信的机制是虚幻的。在这里，基于这样的建议，即由与驱动蛋白头的强相互作用引起的微管蛋白的大构象变化可以沿着微管传播，从而影响远处其他马达的微管蛋白结合能，驱动蛋白-4马达的动力学在从理论上研究了皮摩尔运动浓度，定量解释了实验数据。此外，还从理论上研究了当多个电机在高电机集中度的情况下卡在正端附近时电机的寿命。