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- W2091497253 abstract "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." @default.
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- W2091497253 date "1997-06-09" @default.
- W2091497253 modified "2023-10-17" @default.
- W2091497253 title "Phosphorylation of a 72-kDa protein in PDGF-stimulated cells which forms complex with c-Crk, c-Fyn and Eps15" @default.
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- W2091497253 doi "https://doi.org/10.1016/s0014-5793(97)00495-x" @default.
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