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.
Department of Pathology, University Hospital Case Medical Center, Case Western Reserve University, Cleveland, OH 44106, USA. wenbin.xiao@UHhospitals.org
Wenbin
W
Xiao
Yuko
Y
Kawakami
Toshiaki
T
Kawakami
D000818:Animals; D063646:Carcinogenesis / Q000276:immunology; D019204:GTP-Binding Proteins / Q000276:immunology; D006801:Humans; D007109:Immunity; D056747:Immunomodulation; D046912:Multiprotein Complexes / Q000276:immunology; D022423:Myeloid Cells / Q000201:enzymology; D054799:Phospholipase C beta / Q000737:chemistry / Q000276:immunology*; D020033:Protein Isoforms / Q000737:chemistry / Q000276:immunology; D050799:STAT5 Transcription Factor / Q000276:immunology*; D015398:Signal Transduction / Q000276:immunology; D019061:src-Family Kinases / Q000276:immunology
D046912:Multiprotein Complexes; D020033:Protein Isoforms; D050799:STAT5 Transcription Factor; D019061:src-Family Kinases; D054799:Phospholipase C beta; D019204:GTP-Binding Proteins