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

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.

Pubmed ID: 17567956


  • Dulyaninova NG
  • House RP
  • Betapudi V
  • Bresnick AR


Molecular biology of the cell

Publication Data

August 26, 2007

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM069945
  • Agency: NIGMS NIH HHS, Id: R01 GM069945

Mesh Terms

  • Amino Acid Substitution
  • Casein Kinase II
  • Cell Line, Tumor
  • Cell Movement
  • Epidermal Growth Factor
  • Focal Adhesions
  • Humans
  • Mutant Proteins
  • Myosin Heavy Chains
  • Nonmuscle Myosin Type IIA
  • Phosphorylation
  • Phosphoserine
  • Protein Binding
  • Protein Isoforms
  • Protein Transport
  • Pseudopodia
  • Solubility