Journal of Biological Chemistry · 1997 · 39 citations · 47 references
Life SciencesBiochemistryImmunologyCell SignalingImmunoregulationSignal TransductionCell Surface Receptor SignalingLymphocyte ActivationMembrane ReceptorsReceptor Tyrosine Kinase SignalingReceptor-mediated SignalingC-terminal Src Kinase Binding DomainsExtracellular Signal-regulated Kinase PathwayExtracellular Signal-regulated Kinase SignalingIge Receptor SignalingLyn-mediated SignalingReceptor Affinity RegulationSrc Family ActivationSrc Family Kinases
As an attempt to analyze the roles of C-terminal Src kinase (Csk) in the high affinity IgE receptor (FcepsilonRI)-mediated signaling, we overexpressed Csk, a membrane-targeted form of Csk (mCsk), and a kinase-defective, membrane-targeted form of Csk (mCsk(-)) in rat basophil leukemia (RBL) 2H3 cells. Specific activity of Lyn at the basal state was decreased in Csk-expressing cells, and further decreased in mCsk-expressing cells. In mCsk(-)-expressing cells, basal specific activity of Lyn was increased, thereby indicating that mCsk(-) functioned as a dominant negative molecule. The onset of FcepsilonRI-mediated Lyn activation was delayed in Csk-expressing cells, and further delayed in mCsk-expressing cells. In mCsk(-)-expressing cells, Lyn activation was rapid and quite long lasting. These findings indicate (i) Csk negatively regulates rapid FcepsilonRI/Lyn coupling, and (ii) Csk activity is potentially required for its termination. The onsets of the series of events including tyrosyl phosphorylation of Syk, mitogen-activated protein (MAP) kinase activation, elevation of intracellular calcium concentration ([Ca2+]i), and histamine release were all stepwisely delayed in Csk-expressing cells and in mCsk-expressing cells. The durations of Syk phosphorylation and MAP kinase activation also closely correlated with those of Lyn activation, but [Ca2+]i elevation and histamine release followed different temporal patterns: the delayed responses in Csk-expressing cells and in mCsk-expressing cells led to sustained [Ca2+]i oscillation and histamine release, while the prompt responses in parent cells and mCsk(-)-expressing cells rapidly subsided. These findings provide further evidence that the initiations of the FcepsilonRI-mediated signals are upstreamly regulated by Src family protein tyrosine kinases and revealed that their terminations are regulated by Lyn-dependent (Syk and MAP kinase) and -independent ([Ca2+]i elevation and histamine release) mechanisms.
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cPLA2 is phosphorylated and activated by MAP kinase
Lih‐Ling Lin, Markus Wartmann, Alice Lin et al. · Cell · 1993 · 1.9K citations
Cloning and expression of cDNA for a human thromboxane A2 receptor
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