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

Natalia Dulianinova, Reniqua P. House, Venkaiah Betapudi, Anne R. Bresnick

Research output: Contribution to journalArticle

81 Citations (Scopus)

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
StatePublished - Aug 2007

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Nonmuscle Myosin Type IIA
Myosin Heavy Chains
Phosphorylation
Carcinoma
Epidermal Growth Factor
Chemotaxis
Myosin Type II
Casein Kinase II
Green Fluorescent Proteins
Breast Neoplasms
Wounds and Injuries

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

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Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells. / Dulianinova, Natalia; House, Reniqua P.; Betapudi, Venkaiah; Bresnick, Anne R.

In: Molecular Biology of the Cell, Vol. 18, No. 8, 08.2007, p. 3144-3155.

Research output: Contribution to journalArticle

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