Heregulin and HER2 signaling selectively activates c-Src phosphorylation at tyrosine 215

Ratna K. Vadlamudi, Aysegul A. Sahin, Liana Adam, Rui An Wang, Rakesh Kumar

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

To elucidate the molecular mechanisms by which human epidermal growth factor receptor/heregulin (HER2/HRG) influence the migratory potential of breast cancer cells, we have used phospho-specific antibodies against c-Src kinase and focal adhesion kinase (FAK). This study establishes that HER2/HRG signaling selectively upregulates Tyr phosphorylation of c-Src at Tyr-215 located within the SH2 domain, increases c-Src kinase activity and selectively upregulates Tyr phosphorylation of FAK at Tyr-861. HER2-overexpressing tumors showed increased levels of c-Src phosphorylation at Tyr-215. These findings suggest that HER2/HRG influence metastasis of breast cancer cells through a novel signaling pathway involving phosphorylation of FAK tyrosine 861 via activation of c-Src tyrosine 215.

Original languageEnglish (US)
Pages (from-to)76-80
Number of pages5
JournalFEBS Letters
Volume543
Issue number1-3
DOIs
StatePublished - May 22 2003
Externally publishedYes

Keywords

  • Cytoplasmic tyrosine kinase
  • Growth factor signaling
  • Receptor tyrosine kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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