Computer simulations reveal motor properties generating stable antiparallel microtubule interactions.
An aster of microtubules is a set of flexible polar filaments with dynamic plus ends that irradiate from a common location at which the minus ends of the filaments are found. Processive soluble oligomeric motor complexes can bind simultaneously to two microtubules, and thus exert forces between two asters. Using computer simulations, I have explored systematically the possible steady-state regimes reached by two asters under the action of various kinds of oligomeric motors. As expected, motor complexes can induce the asters to fuse, for example when the complexes consist only of minus end-directed motors, or to fully separate, when the motors are plus end directed. More surprisingly, complexes made of two motors of opposite directionalities can also lead to antiparallel interactions between overlapping microtubules that are stable and sustained, like those seen in mitotic spindle structures. This suggests that such heterocomplexes could have a significant biological role, if they exist in the cell.
Nédélec
François
F
Cell Biology and Biophysics Program, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany. nedelec@embl-heidelberg.de
D000818:Animals; D001696:Biomechanical Phenomena; D003198:Computer Simulation; D003599:Cytoskeleton / Q000378:metabolism; D016547:Kinesins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism* / Q000648:ultrastructure*; D008962:Models, Theoretical; D020409:Molecular Motor Proteins / Q000378:metabolism* / Q000648:ultrastructure*; D011108:Polymers / Q000378:metabolism; D008941:Spindle Apparatus / Q000378:metabolism; D013269:Stochastic Processes; D029867:Xenopus Proteins
C088335:KIF11 protein, Xenopus; D020409:Molecular Motor Proteins; D011108:Polymers; D029867:Xenopus Proteins; D016547:Kinesins