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Vol. 16, Issue 9, 4256-4266, September 2005
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* Department of Biology, Faculty of Science, Yamaguchi University, Yamaguchi 753-8512, Japan;
Department of Physiology and Biophysics, Case School of Medicine, Cleveland, OH 44106-4970; and
Gene Function Research Center, National Institute of Advanced Industrial Science and Technology, Ibaraki 305-8562, Japan
Submitted March 16, 2005;
Revised May 13, 2005;
Accepted June 21, 2005
Monitoring Editor: J. Richard McIntosh
Myosin II filament assembly in Dictyostelium discoideum is regulated via phosphorylation of residues located in the carboxyl-terminal portion of the myosin II heavy chain (MHC) tail. A series of novel protein kinases in this system are capable of phosphorylating these residues in vitro, driving filament disassembly. Previous studies have demonstrated that at least three of these kinases (MHCK A, MHCK B, and MHCK C) display differential localization patterns in living cells. We have created a collection of single, double, and triple gene knockout cell lines for this family of kinases. Analysis of these lines reveals that three MHC kinases appear to represent the majority of cellular activity capable of driving myosin II filament disassembly, and reveals that cytokinesis defects increase with the number of kinases disrupted. Using biochemical fractionation of cytoskeletons and in vivo measurements via fluorescence recovery after photobleaching (FRAP), we find that myosin II overassembly increases incrementally in the mutants, with the MHCK A-/B-/C- triple mutant showing severe myosin II overassembly. These studies suggest that the full complement of MHC kinases that significantly contribute to growth phase and cytokinesis myosin II disassembly in this organism has now been identified.
Address correspondence to: Thomas T. Egelhoff (egelhoff{at}case.edu).
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