A common ATP-dependent stepping model for kinesin-5 and kinesin-1: Mechanism of bi-directionality of kinesin-5

Abstract

Kinesin-5 and kinesin-1 proteins are two families of kinesin superfamily molecular motors that can move processively on microtubules powered by ATP hydrolysis. Kinesin-1 is a unidirectional motor. By contrast, some yeast kinesin-5 motors are bidirectional and the directionality can be switched by changing the experimental conditions. Here, on the basis of a common chemomechanical coupling model, the dynamics of kinesin-1 and in particular the dynamics of kinesin-5 is studied theoretically, explaining the available experimental data. For example, the experimental data about different movement directions under different experimental conditions for kinesin-5 are explained well. The origin of why kinesin-1 can only make unidirectional movement and kinesin-5 can make bidirectional movements is revealed. The origin of mutations or deletions of several structural elements affecting the directionality of kinesin-5 is revealed. Moreover, some predicted results for kinesin-5 are provided.