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Syk 346

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https://www.readbyqxmd.com/read/20828828/syk-and-lyn-mediate-distinct-syk-phosphorylation-events-in-fc%C3%A9-ri-signal-transduction-implications-for-regulation-of-ige-mediated-degranulation
#1
Michael P Sanderson, Eva Wex, Takeshi Kono, Katsuhiro Uto, Andreas Schnapp
Spleen tyrosine kinase (Syk) is a key regulatory factor in the IgE-mediated allergic signal transduction pathway in mast cells and basophils. Syk is phosphorylated on a number of tyrosines following the binding of IgE/allergen complexes to FcɛRI receptors leading to initiation of inflammatory signaling via downstream enzymes and scaffolding proteins. We examined the kinases responsible for the phosphorylation of key Syk tyrosines in rat RBL-2H3 basophilic cells and bone marrow-derived mast cells (BMMCs). The phosphorylation of Syk tyrosine 346 was completely blocked by the novel Src family kinase inhibitor BIRA766, suggesting this tyrosine is a pure substrate for Src family kinases...
November 2010: Molecular Immunology
https://www.readbyqxmd.com/read/12417718/phosphorylation-of-tyr342-in-the-linker-region-of-syk-is-critical-for-fc-epsilon-ri-signaling-in-mast-cells
#2
Juan Zhang, Elsa Berenstein, Reuben P Siraganian
The linker region of Syk and ZAP70 tyrosine kinases plays an important role in regulating their function. There are three conserved tyrosines in this linker region; Tyr317 of Syk and its equivalent residue in ZAP70 were previously shown to negatively regulate the function of Syk and ZAP70. Here we studied the roles of the other two tyrosines, Tyr342 and Tyr346 of Syk, in Fc epsilon RI-mediated signaling. Antigen stimulation resulted in Tyr342 phosphorylation in mast cells. Syk with Y342F mutation failed to reconstitute Fc epsilon RI-initiated histamine release...
December 2002: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/12077122/regulation-of-signaling-in-b-cells-through-the-phosphorylation-of-syk-on-linker-region-tyrosines-a-mechanism-for-negative-signaling-by-the-lyn-tyrosine-kinase
#3
Julie J Hong, Thomas M Yankee, Marietta L Harrison, Robert L Geahlen
The B cell antigen receptor (BCR) is coupled to the mobilization of Ca(2+) by the protein-tyrosine kinase, Syk. Syk, recruited to the clustered BCR, becomes phosphorylated on three tyrosines (Tyr-317, Tyr-342, and Tyr-346) located within the linker region that separates the C-terminal catalytic domain from the N-terminal tandem Src homology 2 domains. Phosphorylation within the linker region can be either activating or inhibitory to Ca(2+) mobilization depending on the sites that are modified. Syk that is not phosphorylated on linker region tyrosines couples the BCR to Ca(2+) mobilization through a phosphoinositide 3-kinase-dependent pathway...
August 30, 2002: Journal of Biological Chemistry
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