Department of Physics, Worcester Polytechnic Institute, Worcester, Massachusetts.
Department of Biophysics, University of Michigan, Ann Arbor, Michigan; Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan.
Biophys J. 2019 Mar 19;116(6):1115-1126. doi: 10.1016/j.bpj.2019.01.036. Epub 2019 Feb 5.
Intracellular cargo transport by kinesin family motor proteins is crucial for many cellular processes, particularly vesicle transport in axons and dendrites. In a number of cases, the transport of specific cargo is carried out by two classes of kinesins that move at different speeds and thus compete during transport. Despite advances in single-molecule characterization and modeling approaches, many questions remain regarding the effect of intermotor tension on motor attachment/reattachment rates during cooperative multimotor transport. To understand the motor dynamics underlying multimotor transport, we analyzed the complexes of kinesin-1 and kinesin-3 motors attached through protein scaffolds moving on immobilized microtubules in vitro. To interpret the observed behavior, simulations were carried out using a model that incorporated motor stepping, attachment/detachment rates, and intermotor force generation. In single-molecule experiments, isolated kinesin-3 motors moved twofold faster and had threefold higher landing rates than kinesin-1. When the positively charged loop 12 of kinesin-3 was swapped with that of kinesin-1, the landing rates reversed, indicating that this "K-loop" is a key determinant of the motor reattachment rate. In contrast, swapping loop 12 had negligible effects on motor velocities. Two-motor complexes containing one kinesin-1 and one kinesin-3 moved at different speeds depending on the identity of their loop 12, indicating the importance of the motor reattachment rate on the cotransport speed. Simulations of these loop-swapped motors using experimentally derived motor parameters were able to reproduce the experimental results and identify best fit parameters for the motor reattachment rates for this geometry. Simulation results also supported previous work, suggesting that kinesin-3 microtubule detachment is very sensitive to load. Overall, the simulations demonstrate that the transport behavior of cargo carried by pairs of kinesin-1 and -3 motors are determined by three properties that differ between these two families: the unloaded velocity, the load dependence of detachment, and the motor reattachment rate.
细胞内货物运输是由驱动蛋白家族的马达蛋白来完成的,这对许多细胞过程至关重要,特别是在轴突和树突中的囊泡运输。在许多情况下,特定货物的运输是由两类移动速度不同的驱动蛋白来完成的,因此在运输过程中存在竞争。尽管在单分子特征描述和建模方法方面取得了进展,但对于在协同多驱动蛋白运输过程中,马达间张力对马达附着/再附着速率的影响,仍有许多问题尚未解决。为了了解多驱动蛋白运输的马达动力学,我们分析了在固定化微管上通过蛋白支架移动的连接在一起的驱动蛋白-1 和驱动蛋白-3 马达复合物。为了解释观察到的行为,我们使用一种模型进行了模拟,该模型包含了马达的步进、附着/脱离速率以及马达间力的产生。在单分子实验中,孤立的驱动蛋白-3 比驱动蛋白-1 移动快两倍,附着率高三倍。当驱动蛋白-3 的正电荷环 12 与驱动蛋白-1 的环 12 交换时,附着率发生了反转,表明这个“K 环”是决定马达再附着速率的关键因素。相比之下,交换环 12 对马达速度几乎没有影响。包含一个驱动蛋白-1 和一个驱动蛋白-3 的双马达复合物以不同的速度移动,这取决于它们的环 12 的身份,这表明马达再附着速率对共运输速度的重要性。使用实验得出的马达参数对这些环交换马达进行模拟,能够重现实验结果,并确定这种几何形状下马达再附着速率的最佳拟合参数。模拟结果还支持了以前的工作,表明驱动蛋白-3 微管的脱离对负载非常敏感。总的来说,模拟结果表明,由驱动蛋白-1 和驱动蛋白-3 组成的货物运输行为由这两种家族之间的三个特性决定:空载速度、脱离的负载依赖性以及马达再附着速率。