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MBC in Press, published online ahead of print June 13, 2007
Mol. Biol. Cell 10.1091/mbc.E06-11-1056

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Submitted on November 30, 2006
Revised on May 30, 2007
Accepted on June 1, 2007

Myosin-IIA Heavy Chain Phosphorylation Regulates the Motility of MDA-MB-231 Carcinoma Cells

Natalya G. Dulyaninova,* Reniqua P. House,* Venkaiah Betapudi,{dagger} and Anne R. Bresnick*

*Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461; {dagger}Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106-4970

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 GFP-myosin-IIA heavy chain S1943E and S1943D mutants displayed increased migration into a wound and enhanced EGF-stimulated lamellipod extension as 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)




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