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

Klaus Hansen; G Alonso; S A Courtneidge; L Rönnstrand; C H Heldin

doi:10.1006/bbrc.1997.7743

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

Klaus Hansen, G Alonso, S A Courtneidge, L Rönnstrand, C H Heldin

17 Citations (Scopus)

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.

Original language	English
Journal	Biochemical and Biophysical Research Communications
Volume	241
Issue number	2
Pages (from-to)	355-62
Number of pages	7
ISSN	0006-291X
DOIs	https://doi.org/10.1006/bbrc.1997.7743
Publication status	Published - 1997

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@article{bf8ce440532511dd8d9f000ea68e967b,

title = "PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation.",

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 = "Klaus Hansen and G Alonso and Courtneidge, {S A} and L R{\"o}nnstrand and Heldin, {C H}",

note = "Keywords: 3T3 Cells; Amino Acid Sequence; Animals; DNA Mutational Analysis; Enzyme Activation; Humans; Mice; Molecular Sequence Data; Peptide Mapping; Phosphorylation; Phosphotyrosine; Platelet-Derived Growth Factor; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-fyn; Receptor Protein-Tyrosine Kinases; Receptor, Platelet-Derived Growth Factor beta; Receptors, Platelet-Derived Growth Factor; Signal Transduction; Tyrosine; src-Family Kinases",

year = "1997",

doi = "10.1006/bbrc.1997.7743",

language = "English",

volume = "241",

pages = "355--62",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

number = "2",

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TY - JOUR

T1 - PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation.

AU - Hansen, Klaus

AU - Alonso, G

AU - Courtneidge, S A

AU - Rönnstrand, L

AU - Heldin, C H

N1 - Keywords: 3T3 Cells; Amino Acid Sequence; Animals; DNA Mutational Analysis; Enzyme Activation; Humans; Mice; Molecular Sequence Data; Peptide Mapping; Phosphorylation; Phosphotyrosine; Platelet-Derived Growth Factor; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-fyn; Receptor Protein-Tyrosine Kinases; Receptor, Platelet-Derived Growth Factor beta; Receptors, Platelet-Derived Growth Factor; Signal Transduction; Tyrosine; src-Family Kinases

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

U2 - 10.1006/bbrc.1997.7743

DO - 10.1006/bbrc.1997.7743

M3 - Journal article

C2 - 9425276

SN - 0006-291X

VL - 241

SP - 355

EP - 362

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

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

Abstract

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