Long-Range Coupling between Kinesins Regulates Collective Motor Behavior

Coupling of motor proteins within large arrays drives muscle contraction, flagellar beating, chromosome segregation, and other biological processes. Short-range interaction mechanisms coupling, such as steric crowding mechanical linkage, have been well-studied. However, coupling that act at longer length scales remain largely unexplored. Here we report evidence long-range motor-motor on microtubules picomolar protein concentration, where short-range interactions are unlikely. We find the human kinesin-4 Kif4A changes processivity velocity motors same microtubule in a dose-dependent manner, even low density. Similar motility can be induced by kinesin-1 microtubule. A micron-scale attractive potential between kinesin is sufficient to recreate experimental results kinetic Monte Carlo simulation. model which alters not just binding-unbinding kinetics but also modifies mechanochemical cycle better fits data. Given long scale interaction, natural medium couple motors, possibly via motor-induced lattice deformation. These suggest paradigm lattice, rather than being merely passive track, dynamic responsive binding enable new forms collective behavior.