Epidermal growth factor-induced activation and translocation of c-Src to the cytoskeleton depends on the actin binding domain of the EGF-receptor

Marcel A.G. Van Der Heyden, Paschal A. Oude Weernink, Brigitte A. Van Oirschot, Paul M.P. Van Bergen En Henegouwen, Johannes Boonstra, Gert Rijksen*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

11 Citations (Scopus)

Abstract

In the epidermal growth factor (EGF)-receptor signal transduction cascade, the non-receptor tyrosine kinase c-Src has been demonstrated to become activated upon EGF stimulation. In this paper we show that c-Src associates with the cytoskeleton and co-isolates with the actin filaments upon EGF treatment of NIH-3T3 cells transfected with the EGF receptor. Immunofluorescence studies using CLSM show colocalization of F-actin and endogenous c-Src predominantly around endosomes and not on stress fibers and cell-cell contacts. Stimulation of EGF receptor-transfected NIH-3T3 cells with EGF induces an activation and translocation of c-Src to the cytoskeleton. These process depend upon the presence of the actin binding domain of the EGF-receptor since in cells that express EGF-receptors lacking this domain, EGF fails to induce an activation and translocation to the cytoskeleton of c-Src. These data suggest a role for the actin binding domain of the EGF-receptor in the translocation of c-Src.

Original languageEnglish
Pages (from-to)211-221
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1359
Issue number3
DOIs
Publication statusPublished - 12 Dec 1997
Externally publishedYes

Keywords

  • Actin
  • c-SRC
  • Cytoskeleton
  • Epidermal growth factor receptor

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