Phosphoinositide-specific phospholipase C (PLC) plays a critical role in the initiation of receptor mediated signal transduction through the generation of the two second messengers, inositol 1,4,5-triphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. PLCγ2 associates with several tyrosine-phosphorylated proteins (Syk, SLP-76, Lyn, linker for activation of T cells (LAT) and the FcR chain), which bind to its C-terminal SH2 domain. The C-terminal SH2 domain is involved in the regulation of PLCγ2. In addition, Btk can induce PLCγ2 tyrosine phosphorylation and initiate calcium moblization in CD72-stimulated B lymphocytes.
