PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation
Författare
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.
Publiceringsår
1997
Språk
Engelska
Sidor
355-362
Publikation/Tidskrift/Serie
Biochemical and Biophysical Research Communications
Volym
241
Issue
2
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Ämne
- Medicinal Chemistry
Nyckelord
- 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/Övrigt
- ISSN: 1090-2104