An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism

The conventional kinesin (kinesin-1) molecular motor is a prototypical member of the kinesin superfamily. It can processively step on microtubules toward the plus end by hydrolyzing ATP molecules, performing the biological function of shuttling cargos in cells. Its dynamics have been thoroughly studied using various methods including biochemical measurement, single molecule imaging, single molecule optical trapping, and so on. While most of the experiments yielded consistent results on the dynamics of the motor, a lot of conflicting experimental results have also been presented. Here, a brief review is given of the diverse conflicting experimental results. Furthermore, a model for the chemomechanical coupling of the motor is briefly reviewed, which can consistently and quantitatively explain these conflicting experimental results in addition to the other experimental results. A consistent explanation of the diverse conflicting experimental results with the same model is an essential criterion for determining the correctness of the model.