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Vol. 10, Issue 5, 1309-1323, May 1999
Department of Biology and Institute for Biomedical Computing,
Washington University, Box 1229, St. Louis, Missouri 63130
To investigate myosin II function in cell movement within a cell
mass, we imaged green fluorescent protein-myosin heavy chain (GFP-MHC)
cells moving within the tight mound of Dictyostelium discoideum. In the posterior cortex of cells undergoing
rotational motion around the center of the mound, GFP-MHC cyclically
formed a "C," which converted to a spot as the cell retracted its
rear. Consistent with an important role for myosin in rotation, cells failed to rotate when they lacked the myosin II heavy chain
(MHC
) or when they contained predominantly monomeric
myosin II (3xAsp). In cells lacking the myosin II regulatory light
chain (RLC), rotation was impaired and eventually ceased.
These rotational defects reflect a mechanical problem in the 3xAsp and
RLC cells, because these mutants exhibited proper
rotational guidance cues. MHC cells exhibited
disorganized and erratic rotational guidance cues, suggesting a
requirement for the MHC in organizing these signals. However, the
MHC cells also exhibited mechanical defects in rotation,
because they still moved aberrantly when seeded into wild-type mounds with proper rotational guidance cues. The mechanical defects in rotation may be mediated by the C-to-spot, because
RLC cells exhibited a defective C-to-spot, including a
slower C-to-spot transition, consistent with this mutant's slower
rotational velocity.
Online version contains video material for Figures 1,
2, and 5. Online version available at www.molbiolcell.org.
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