Immune regulation by phospholipase C-β isoforms.

Rapid progress has recently been made regarding how phospholipase C (PLC)-β functions downstream of G protein-coupled receptors and how PLC-β functions in the nucleus. PLC-β has also been shown to interplay with tyrosine kinase-based signaling pathways, specifically to inhibit Stat5 activation by recruiting the protein-tyrosine phosphatase SHP-1. In this regard, a new multimolecular signaling platform, named SPS complex, has been identified. The SPS complex has important regulatory roles in tumorigenesis and immune cell activation. Furthermore, a growing body of work suggests that PLC-β also participates in the differentiation and activation of immune cells that control both the innate and adaptive immune systems.