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

Hansen, Klaus; Alonso, Gema; Courtneidge, Sara A; Rönnstrand, Lars LU and Heldin, Carl-Henrik (1997) In Biochemical and Biophysical Research Communications 241(2). p.355-362
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.
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author
publishing date
type
Contribution to journal
publication status
published
subject
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
in
Biochemical and Biophysical Research Communications
volume
241
issue
2
pages
355 - 362
publisher
Elsevier
external identifiers
  • Scopus:0031577713
ISSN
1090-2104
DOI
10.1006/bbrc.1997.7743
language
English
LU publication?
no
id
fbfe36f0-797e-4715-92a2-3c627e46745a (old id 1783940)
date added to LUP
2011-02-07 15:49:44
date last changed
2016-10-13 04:33:24
@misc{fbfe36f0-797e-4715-92a2-3c627e46745a,
  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.},
  author       = {Hansen, Klaus and Alonso, Gema and Courtneidge, Sara A and Rönnstrand, Lars and Heldin, Carl-Henrik},
  issn         = {1090-2104},
  keyword      = {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},
  language     = {eng},
  number       = {2},
  pages        = {355--362},
  publisher    = {ARRAY(0xd73b030)},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation},
  url          = {http://dx.doi.org/10.1006/bbrc.1997.7743},
  volume       = {241},
  year         = {1997},
}