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A more recent version of this article appeared on October 1, 2006
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Submitted on May 22, 2006
Revised on July 3, 2006
Accepted on July 10, 2006
Department of Pathology and Anatomical Sciences, Division of Anatomy and Cell Biology, State University of New York at Buffalo School of Medicine and Biomedical Sciences, Buffalo, New York 14214
Monitoring Editor: Paul Forscher
Nonmuscle myosin IIA and IIB distribute preferentially toward opposite ends of migrating endothelial cells. To understand the mechanism and function of this behavior, myosin II was examined in cells treated with the motor inhibitor, blebbistatin. 
30 µM blebbistatin inhibited anterior redistribution of myosin IIA, with 100 µM blebbistatin causing posterior accumulation. Posterior accumulation of myosin IIB was unaffected. Time-lapse cinemicrography showed myosin IIA entering lamellipodia shortly after their formation, but failing to move into lamellipodia in blebbistatin. Thus, myosin II requires motor activity to move forward onto F-actin in protrusions. However, this movement is inhibited by myosin filament assembly, as whole myosin was delayed relative to a tailless fragment. Inhibiting myosin’s forward movement reduced coupling between protrusive activity and translocation of the cell body: In untreated cells, body movement followed advancing lamellipodia, whereas blebbistatin-treated cells extended protrusions without displacement of the body or with a longer delay before movement. Anterior cytoplasm of blebbistatin-treated cells contained disorganized bundles of parallel microfilaments, but anterior F-actin bundles in untreated cells were mostly oriented perpendicular to movement. Myosin II may ordinarily move anteriorly on actin filaments and pull cross-ed filaments into anti-parallel bundles, with the resulting realignment pulling the cell body forward.
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