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Phospholipase C gamma 2 1217

Lisa A Humphries, Carol Dangelmaier, Karen Sommer, Kevin Kipp, Roberta M Kato, Natasha Griffith, Irene Bakman, Christoph W Turk, James L Daniel, David J Rawlings
Tyrosine phosphorylation of phospholipase Cgamma2 (PLCgamma2) is a crucial activation switch that initiates and maintains intracellular calcium mobilization in response to B cell antigen receptor (BCR) engagement. Although members from three distinct families of non-receptor tyrosine kinases can phosphorylate PLCgamma in vitro, the specific kinase(s) controlling BCR-dependent PLCgamma activation in vivo remains unknown. Bruton's tyrosine kinase (Btk)-deficient human B cells exhibit diminished inositol 1,4,5-trisphosphate production and calcium signaling despite a normal inducible level of total PLCgamma2 tyrosine phosphorylation...
September 3, 2004: Journal of Biological Chemistry
D Watanabe, S Hashimoto, M Ishiai, M Matsushita, Y Baba, T Kishimoto, T Kurosaki, S Tsukada
Activation of phospholipase C-gamma2 (PLCgamma2) is the critical step in B cell antigen receptor (BCR)-coupled calcium signaling. Although genetic dissection experiments on B cells have demonstrated that Bruton's tyrosine kinase (Btk) and Syk are required for activating PLCgamma2, the exact activation mechanism of PLCgamma2 by these kinases has not been established. We identify the tyrosine residues 753, 759, 1197, and 1217 in rat PLCgamma2 as Btk-dependent phosphorylation sites by using an in vitro kinase assay...
October 19, 2001: Journal of Biological Chemistry
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