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- W4313335879 abstract "Abstract The protein tyrosine kinase Syk is an essential element in several cascades coupling Ag receptors to cell responses. Syk and the mitogen-activated protein kinase extracellular signal-regulated kinase 1 (ERK1) were found to form a tight complex in both resting and Ag-stimulated rat mucosal-type mast cells (rat basophilic leukemia 2H3 cell line RBL-2H3). A direct serine phosphorylation and activation of Syk by ERK was observed in in vitro experiments. Moreover the mitogen-activated protein kinase/extracellular signal-regulated protein kinase (ERK) kinase (MEK) inhibitors markedly decreased the Ag-induced phosphorylation of the tyrosyl residues of Syk and its activation as well as suppressed the degranulation of the cells. These results suggest a positive feedback regulation of Syk by ERK in the cascade coupling the type 1 Fcε receptor to the secretory response of mast cells; hence, the existence of a novel type of cross-talk between protein serine/threonine kinases and protein tyrosine kinases is suggested." @default.
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- W4313335879 date "1999-08-01" @default.
- W4313335879 modified "2023-10-15" @default.
- W4313335879 title "Cutting Edge: Extracellular Signal-Regulated Kinase Activates Syk: A New Potential Feedback Regulation of Fcε Receptor Signaling" @default.
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- W4313335879 doi "https://doi.org/10.4049/jimmunol.163.3.1110" @default.
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