PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation

Klaus Hansen, Gema Alonso, Sara A. Courtneidge, Lars Rönnstrand, Carl Henrik Heldin

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Binding of platelet-derived growth factor (PDGF) to its receptors leads to the activation of members of the Src family of protein tyrosine kinases. We show here that Fyn, a member of the Src family, is phosphorylated on Tyr28 in the unique N-terminal part of the molecule after interaction with the intracellular domain of the PDGP β-receptor. Activated Fyn furthermore undergoes autophosphorylation on Tyr30, Tyr39 and Tyr420. When Fyn mutants with Tyr28, Tyr30 or Tyr39 replaced with phenylalanine residues were transfected into NIH3T3 cells a decreased activation after PDGF stimulation was seen, suggesting a functional importance of the N-terminal tyrosine phosphorylation of Fyn.

Original languageEnglish (US)
Pages (from-to)355-362
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume241
Issue number2
DOIs
StatePublished - Dec 18 1997

    Fingerprint

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this