Local signaling by the EGF receptor

J Cell Biol. 2003 Sep 1;162(5):781-7. doi: 10.1083/jcb.200303144.

Abstract

Differing spatial scales of signaling cascades are critical for cell orientation during chemotactic responses. We used biotin EGF bound to streptavidin-coupled magnetic beads to locally stimulate cells overexpressing the EGF receptor. We have found that EGF-induced actin polymerization remains localized even under conditions of receptor overexpression. Conversely, EGF-induced ERK activation spreads throughout the cell body after EGF bead stimulation. The localized actin polymerization is independent of PI3-kinase and rho protein activity and requires Arp2/3 complex and cofilin function. Thus, we find differing spatial scales of signaling from the EGF receptor, supporting models of chemotaxis that integrate short- and long-range signaling.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actin Depolymerizing Factors
  • Actins / metabolism
  • Androstadienes / metabolism
  • Animals
  • Cell Line, Tumor
  • Enzyme Inhibitors / metabolism
  • Epidermal Growth Factor / metabolism
  • ErbB Receptors / metabolism*
  • Humans
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • Mitogen-Activated Protein Kinases / metabolism
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphotyrosine / metabolism
  • Protein Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-akt
  • RNA, Small Interfering / metabolism
  • Rats
  • Signal Transduction / physiology*
  • Wortmannin

Substances

  • Actin Depolymerizing Factors
  • Actins
  • Androstadienes
  • Enzyme Inhibitors
  • Microfilament Proteins
  • Proto-Oncogene Proteins
  • RNA, Small Interfering
  • Phosphotyrosine
  • Epidermal Growth Factor
  • ErbB Receptors
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • Mitogen-Activated Protein Kinases
  • Wortmannin