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Vol. 18, Issue 8, 3144-3155, August 2007
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*Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461; and Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106-4970
Submitted November 30, 2006;
Revised May 30, 2007;
Accepted June 1, 2007
Monitoring Editor: Yu-li Wang
In mammalian nonmuscle cells, the mechanisms controlling the localized formation of myosin-II filaments are not well defined. To investigate the mechanisms mediating filament assembly and disassembly during generalized motility and chemotaxis, we examined the EGF-dependent phosphorylation of the myosin-IIA heavy chain in human breast cancer cells. EGF stimulation of MDA-MB-231 cells resulted in transient increases in both the assembly and phosphorylation of the myosin-IIA heavy chains. In EGF-stimulated cells, the myosin-IIA heavy chain is phosphorylated on the casein kinase 2 site (S1943). Cells expressing green fluorescent protein-myosin-IIA heavy-chain S1943E and S1943D mutants displayed increased migration into a wound and enhanced EGF-stimulated lamellipod extension compared with cells expressing wild-type myosin-IIA. In contrast, cells expressing the S1943A mutant exhibited reduced migration and lamellipod extension. These observations support a direct role for myosin-IIA heavy-chain phosphorylation in mediating motility and chemotaxis.
Address correspondence to: Anne R. Bresnick (bresnick{at}aecom.yu.edu).
Abbreviations used: NMHC-IIA, nonmuscle myosin-IIA heavy chain; NMHC-IIB, nonmuscle myosin-IIB heavy chain; RLC, regulatory light chain; GFP, green fluorescent protein; CK2, casein kinase 2; PKC, protein kinase C.
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