Induction of tyrosine phosphorylation and translocation of ezrin by hepatocyte growth factor/scatter factor

Biochem Biophys Res Commun. 1995 Dec 26;217(3):1062-9. doi: 10.1006/bbrc.1995.2877.


Ezrin is a member of the TERM family and is a key protein in cytoplasmic membrane-cytoskeleton interactions. This study showed that hepatocyte growth factor/scatter factor (HGF/SF), a cytokine known to regulate motility, morphogenesis and growth of cells, stimulated the tyrosine phosphorylation of ezrin in a human colon epithelial cell line, HT115. After HGF/SF stimulation, ezrin translocated from the cytosol and generalised membrane to the areas of ruffled membrane as visualised by indirect immunofluorescent and immunogold electron microscopy. This effect was inhibited by genistein, a tyrosine kinase inhibitor. It is concluded that HGF/SF induces ezrin translocation by stimulation of its tyrosine phosphorylation and that this plays a key role in HGF/SF induced membrane ruffling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Cell Compartmentation
  • Cell Membrane / ultrastructure
  • Cytoskeletal Proteins
  • Enzyme Inhibitors / pharmacology
  • Genistein
  • Hepatocyte Growth Factor / physiology*
  • Humans
  • Immunohistochemistry
  • Isoflavones / pharmacology
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Phosphotyrosine / metabolism*
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Tumor Cells, Cultured


  • Actins
  • Cytoskeletal Proteins
  • Enzyme Inhibitors
  • Isoflavones
  • Phosphoproteins
  • ezrin
  • Phosphotyrosine
  • Hepatocyte Growth Factor
  • Genistein
  • Protein-Tyrosine Kinases