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CUTTING EDGE |
Receptor Signaling1
Departments of
*
Immunology and
Biological Regulation, The Weizmann Institute of Science, Rehovot, Israel
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 Fc
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.
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