Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells

Natalya G. Dulyaninova, Reniqua P. House, Venkaiah Betapudi, Anne R. Bresnick

Research output: Contribution to journalArticle

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)3144-3155
Number of pages12
JournalMolecular biology of the cell
Volume18
Issue number8
DOIs
Publication statusPublished - Aug 1 2007

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ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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