Collective behavior of antagonistically acting kinesin-1 motors.
In many subcellular force-generating systems, groups of motor proteins act antagonistically. Here, we present an experimental study of the tug of war between superprocessive kinesin-1 motors acting on antiparallel microtubule doublets in vitro. We found distinct modes of slow and fast movements, as well as sharp transitions between these modes and regions of coexistence. We compare our experimental results to a quantitative theory based on the physical properties of individual motors. Our results show that mechanical interactions between motors can collectively generate coexisting transport regimes with distinct velocities.
Leduc
Cecile
C
Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.
Pavin
Nenad
N
Jülicher
Frank
F
Diez
Stefan
S
D001692:Biological Transport; D001703:Biophysics; D002465:Cell Movement; D016547:Kinesins / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D008856:Microscopy, Fluorescence; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism
D020409:Molecular Motor Proteins; D016547:Kinesins