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

På svenska

Author

  • Klaus Hansen
  • Gema Alonso
  • Sara A Courtneidge
  • Lars Rönnstrand
  • Carl-Henrik Heldin

Summary, in English

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 PDGF beta-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.

Publishing year

1997

Language

English

Pages

355-362

Publication/Series

Biochemical and Biophysical Research Communications

Volume

241

Issue

2

Document type

Journal article

Publisher

Elsevier

Topic

  • Medicinal Chemistry

Keywords

  • Platelet-Derived Growth Factor beta Receptors
  • 3T3 Cells Amino Acid Sequence Animals DNA Mutational Analysis Enzyme Activation/genetics Humans Mice Molecular Sequence Data Peptide Mapping Phosphorylation Phosphotyrosine/biosynthesis Platelet-Derived Growth Factor/*pharmacology Proto-Oncogene Proteins/genetics/*metabolism Proto-Oncogene Proteins c-fyn Receptor Protein-Tyrosine Kinases/*metabolism Receptor
  • Platelet-Derived Growth Factor/*metabolism Signal Transduction Tyrosine/metabolism src-Family Kinases/genetics/*metabolism

Status

Published

ISBN/ISSN/Other

  • ISSN: 1090-2104