Thomas G M, Cunningham E, Fensome A, Ball A, Totty N F, Truong O, Hsuan J J, Cockcroft S
Department of Physiology, University College London, England.
Cell. 1993 Sep 10;74(5):919-28. doi: 10.1016/0092-8674(93)90471-2.
Transmembrane signaling by the phospholipase C-beta (PLC-beta) pathway is known to require at least three components: the receptor, the G protein, and the PLC. Recent studies have indicated that if the cytosol is allowed to leak out of HL60 cells, then G protein-stimulated PLC activity is greatly diminished, indicating an essential role for a cytosolic component(s). We now report the complete purification of one component based on its ability to reconstitute GTP gamma S-mediated PLC activity and identify it as the phosphatidylinositol transfer protein (PI-TP). Based on the in vitro effects of PI-TP, we surmise that it is involved in transporting PI from intracellular compartments for conversion to PI bisphosphate (PIP2) prior to hydrolysis by PLC-beta 2/PLC-beta 3, the endogenous PLC isoforms present in these cells.
已知磷脂酶C-β(PLC-β)途径的跨膜信号传导至少需要三个组件:受体、G蛋白和PLC。最近的研究表明,如果允许HL60细胞的胞质溶胶泄漏,那么G蛋白刺激的PLC活性会大大降低,这表明胞质组分具有重要作用。我们现在报告基于其重建GTPγS介导的PLC活性的能力对一种组分进行了完全纯化,并将其鉴定为磷脂酰肌醇转移蛋白(PI-TP)。基于PI-TP的体外作用,我们推测它参与将PI从细胞内区室转运出来,以便在被这些细胞中存在的内源性PLC同工型PLC-β2/PLC-β3水解之前转化为磷脂酰肌醇二磷酸(PIP2)。