| Literature DB >> 23981313 |
Toshiaki Kawakami1, Wenbin Xiao.
Abstract
Great progress has recently been made in structural and functional research of phospholipase C (PLC)-β. We now understand how PLC-β isoforms (β1-β4) are activated by GTP-bound Gαq downstream of G protein-coupled receptors. Numerous studies indicate that PLC-βs participate in the differentiation and activation of immune cells that control both the innate and adaptive immune systems. The PLC-β3 isoform also interplays with tyrosine kinase-based signaling pathways, to inhibit Stat5 activation by recruiting the protein-tyrosine phosphatase SHP-1, with which PLC-β3 and Stat5 form a multi-molecular signaling platform, named SPS complex. The SPS complex has important regulatory roles in tumorigenesis and immune cell activation.Entities:
Keywords: B cell receptor; BCR; C-terminal; CT; DAG; G-protein-coupled receptor; GAP; GPCR; GTPase-activating protein; HSC; IL; IP(3); ITAM; NP; PG; PKC; PLC; SH2; Src homology 2; T cell receptor; T cell-independent; TCR; TI; TNFα; diacylglycerol; dko; double knockout; hematopoietic stem cell; hydroxylnitrophenyl; immunoreceptor tyrosine-based activation motif; inositol 1,4,5-trisphosphate; interleukin; phospholipase C; prostaglandin; protein kinase C; tumor necrosis factor α
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Year: 2013 PMID： 23981313 PMCID： PMC4324595 DOI： 10.1016/j.jbior.2013.08.001
Source DB: PubMed Journal: Adv Biol Regul ISSN： 2212-4926