PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1783940
- author
- Hansen, Klaus ; Alonso, Gema ; Courtneidge, Sara A ; Rönnstrand, Lars LU and Heldin, Carl-Henrik
- publishing date
- 1997
- 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}}, }