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Phosphorylation of a 72‐kDa protein in PDGF‐stimulated cells which forms complex with c‐Crk, c‐Fyn and Eps15
Author(s) -
Hansen Klaus,
Rönnstrand Lars,
Claesson-Welsh Lena,
Heldin Carl-Henrik
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00495-x
Subject(s) - adapter molecule crk , platelet derived growth factor receptor , microbiology and biotechnology , fyn , tyrosine phosphorylation , phosphorylation , receptor tyrosine kinase , signal transducing adaptor protein , proto oncogene tyrosine protein kinase src , tyrosine kinase , biology , signal transduction , sh2 domain , chemistry , receptor , biochemistry , growth factor
Ligand‐induced activation of the β ‐receptor for platelet‐derived growth factor (PDGF) induces tyrosine phosphorylation of a number of downstream signaling proteins. In the present study, we used two‐dimensional gel electrophoresis to characterize the spectrum of proteins phosphorylated in response to PDGF stimulation in porcine aortic endothelial cells expressing PDGF β ‐receptors. Several previously known substrates for the PDGF β ‐receptor were identified as well as a novel substrate of 72 kDa. The 72‐kDa component could be co‐immunoprecipitated in complex with the adaptor protein c‐Crk, the non‐receptor tyrosine kinase c‐Fyn and the signaling molecule Eps15. The results obtained suggests that the 72‐kDa protein might play an important role in signaling via the PDGF β ‐receptor, coupling non‐receptor tyrosine kinases of the Src family with c‐Crk and Eps15.