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Biochem Biophys Res Commun. 1997 Dec 18;241(2):355-62.

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

Author information

1
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.

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 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.

PMID:
9425276
DOI:
10.1006/bbrc.1997.7743
[Indexed for MEDLINE]

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