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Vol. 8, Issue 12, 2605-2615, December 1997
Department of Biochemistry, Stanford University School of Medicine,
Stanford, CA 94305
Conventional myosin II plays a fundamental role in the
process of cytokinesis where, in the form of bipolar thick filaments, it is thought to be the molecular motor that generates the force necessary to divide the cell. In Dictyostelium, the
formation of thick filaments is regulated by the phosphorylation of
three threonine residues in the tail region of the myosin heavy chain. We report here on the effects of this regulation on the localization of
myosin in live cells undergoing cytokinesis. We imaged fusion proteins
of the green-fluorescent protein with wild-type myosin and with myosins
where the three critical threonines had been changed to either alanine
or aspartic acid. We provide evidence that thick filament formation is
required for the accumulation of myosin in the cleavage furrow and that
if thick filaments are overproduced, this accumulation is markedly
enhanced. This suggests that myosin localization in dividing cells is
regulated by myosin heavy chain phosphorylation.
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