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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 orcid 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
; ; ; and
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
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
id
fbfe36f0-797e-4715-92a2-3c627e46745a (old id 1783940)
date added to LUP
2016-04-04 09:35:29
date last changed
2022-03-15 20:02:23
@article{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}},
  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}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{355--362}},
  publisher    = {{Elsevier}},
  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}},
  doi          = {{10.1006/bbrc.1997.7743}},
  volume       = {{241}},
  year         = {{1997}},
}