Molecular mechanism of interaction between kinesin motors affecting their residence times on microtubule lattice and end.

Kinesin superfamily can be classified into 14 subfamilies. Some families of kinesin motors such as kinesin-1 are responsible for long-distance intracellular transports and thus the motors are required to reside on the microtubule (MT) lattice for a longer time than at the end. Some families such as kinesin-8 Kip3 and kinesin-5 Eg5 are responsible for the regulation of MT length by depolymerizing or polymerizing the MT from the plus end and thus the motors are required to reside at the MT end for a long time. Under the crowded condition of the motors, it was found experimentally that the residence times of the kinesin-8 Kip3 and kinesin-5 Eg5 at the MT end are reduced greatly compared to the single-motor case. However, the underlying mechanism of different families of kinesin motors having different MT-end residence times is unknown. The molecular mechanism by which the interaction between the two motors greatly reduces the residence time of the motor at the MT end is elusive. In addition, during the processive stepping on the MT lattice, when two kinesin motors meet it is unknown how the interaction between them affects their dissociation rates. To address the above unclear issues, here we make a consistent and theoretical study of the residence times of the kinesin-1, kinesin-8 Kip3 and kinesin-5 Eg5 motors on the MT lattice and at the end under both the single-motor condition and multiple-motors or crowded condition.