Key result
Dictyostelium cells lacking different myosin I pairs redistributed their F-actin more slowly than wild type cells upon adhesion to a substrate.
Dictyostelium myoA, myoB, and myoC may have overlapping roles in maintaining the integrity or organization of the cortical membrane cytoskeleton.
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Slower F-actin redistribution in myosin I knockouts; leaves open relevance to human cardiac cytoskeletal dynamics.
The roles of the myosin I class of mechanoenzymes have been investigated by single and double gene knockout studies in the amoeba Dictyostelium discoideum. Cells lacking different myosin I pairs (myoA-/myoB-, myoB-/myoC-, and myoA-/myoC-) were examined with respect to their cytoskeletal organization. F-actin localization by rhodamine-phalloidin staining of cells indicates that the myoA-/myoB-, myoB-/myoC-, and myoA-/myoC- cells appear to redistribute their F-actin more slowly than wild type cells upon adhesion to a substrate. These studies suggest that Dictyostelium myoA, myoB, and myoC may have overlapping roles in maintaining the integrity or organization of the cortical membrane cytoskeleton.
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Peterson et al. (1994) studied this question. Myosin I double gene knockouts (myoA-/myoB-, myoB-/myoC-, and myoA-/myoC-) vs. Wild type cells was evaluated on F-actin localization and redistribution upon adhesion to a substrate. Dictyostelium cells lacking different myosin I pairs redistributed their F-actin more slowly than wild type cells upon adhesion to a substrate.
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