Impaired c-src activation and motility defects in PEA3-null fibroblasts

Biochim Biophys Acta. 2012 Dec;1823(12):2237-42. doi: 10.1016/j.bbamcr.2012.09.002. Epub 2012 Sep 12.

Abstract

Null mutations in the pea3 allele compromise the capacity of mammary tumors to metastasize in MMTV-Neu/ErbB2/HER2 transgenic mice, indicating a motility defect in PEA3-null cells. Cellular and biochemical analyses of established PEA3-null fibroblasts show impaired motility and aberrant localization of adhesion proteins in spreading cells. Our results show that PEA3-/- cells express normal levels of key adhesion components, but that spreading PEA3-null cells fail to activate c-src and to downregulate phospho-FAK(Y397), suggesting that focal adhesion signaling is impaired. Supporting this, biochemical analysis revealed that adhesion complex-associated proteins such as p130Cas failed to undergo tyrosine phosphorylation and dissociated from the adhesion complex with delayed kinetics. Overall our data show that the motility defects observed in PEA3-null cells are due to altered adhesion signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Cell Movement / physiology*
  • Cells, Cultured
  • Crk-Associated Substrate Protein / metabolism*
  • Embryo, Mammalian / cytology
  • Embryo, Mammalian / metabolism
  • Female
  • Fibroblasts / cytology
  • Fibroblasts / metabolism*
  • Fibronectins / pharmacology
  • Fluorescent Antibody Technique
  • Focal Adhesions / physiology
  • Genes, src / physiology*
  • Immunoprecipitation
  • Mammary Tumor Virus, Mouse / genetics
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Phosphorylation
  • Receptor, ErbB-2 / genetics
  • Signal Transduction
  • Transcription Factors / physiology*
  • Tyrosine / metabolism

Substances

  • Bcar1 protein, mouse
  • Crk-Associated Substrate Protein
  • Fibronectins
  • Transcription Factors
  • transcription factor PEA3
  • Tyrosine
  • Receptor, ErbB-2