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Biopolymers serve as one-dimensional tracks on which motor proteins move toperform their biological roles. Motor protein phenomena have inspiredtheoretical models of one-dimensional transport, crowding, and jamming.Experiments studying the motion of Xklp1 motors on reconstituted antiparallelmicrotubule overlaps demonstrated that motors recruited to the overlap walktoward the plus end of individual microtubules and frequently switch betweenfilaments. We study a model of this system that couples the totally asymmetricsimple exclusion process (TASEP) for motor motion with switches betweenantiparallel filaments and binding kinetics. We determine steady-state motordensity profiles for fixed-length overlaps using exact and approximatesolutions of the continuum differential equations and compare to kinetic MonteCarlo simulations. Overlap motor density profiles and motor trajectoriesresemble experimental measurements. The phase diagram of the model is similarto the single-filament case for low switching rate, while for high switchingrate we find a new low density-high density-low density-high density phase. Theoverlap center region, far from the overlap ends, has a constant motor densityas one would naively expect. However, rather than following a simple bindingequilibrium, the center motor density depends on total overlap length, motorspeed, and motor switching rate. The size of the crowded boundary layer nearthe overlap ends is also dependent on the overlap length and switching rate inaddition to the motor speed and bulk concentration. The antiparallelmicrotubule overlap geometry may offer a previously unrecognized mechanism forbiological regulation of protein concentration and consequent activity.

Motor protein accumulation on antiparallel microtubule overlaps