Highly loaded behavior of kinesins increases the robustness of transport under high resisting loads.
Kinesins are nano-sized biological motors which walk by repeating a mechanochemical cycle. A single kinesin molecule is able to transport its cargo about 1 μm in the absence of external loads. However, kinesins perform much longer range transport in cells by working collectively. This long range of transport by a team of kinesins is surprising because the motion of the cargo in cells can be hindered by other particles. To reveal how the kinesins are able to accomplish their tasks of transport in harsh intracellular circumstances, stochastic studies on the kinesin motion are performed by considering the binding and unbinding of kinesins to microtubules and their dependence on the force acting on kinesin molecules. The unbinding probabilities corresponding to each mechanochemical state of kinesin are modeled. The statistical characterization of the instants and locations of binding are captured by computing the probability of unbound kinesin being at given locations. It is predicted that a group of kinesins has a more efficient transport than a single kinesin from the perspective of velocity and run length. Particularly, when large loads are applied, the leading kinesin remains bound to the microtubule for long time which increases the chances of the other kinesins to bind to the microtubule. To predict effects of this behavior of the leading kinesin under large loads on the collective transport, the motion of the cargo is studied when the cargo confronts obstacles. The result suggests that the behavior of kinesins under large loads prevents the early termination of the transport which can be caused by the interference with the static or moving obstacles.
Department of Mechanical Engineering, University of Michigan, Ann Arbor, Michigan, United States of America.
Woochul
W
Nam
Department of Mechanical Engineering, University of Michigan, Ann Arbor, Michigan, United States of America.
Bogdan I
BI
Epureanu
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D001696:Biomechanical Phenomena; D019295:Computational Biology; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D011188:Potassium / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding
D000255:Adenosine Triphosphate; D016547:Kinesins; D011188:Potassium