Activation of phosphatidylinositol lipid-specific phospholipase C-beta 3 by G-protein beta gamma subunits.
A novel member of the inositol lipid-specific phospholipase C family, PtdIns-PLC beta 3, is shown to be activated by beta gamma subunits of the heterotrimeric GTP-binding protein, transducin. The activation is a direct effect since it is observed with the purified proteins. Furthermore, the activation is blocked by the GDP-liganded alpha subunit of transducin, confirming that the effect is due to free beta gamma subunits. The implications with respect to receptor-PtdIns-PLC coupling are discussed.
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London, UK.
A
A
Carozzi
M
M
Camps
P
P
Gierschik
P J
PJ
Parker
D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D002461:Cell Line, Transformed; D002522:Chlorocebus aethiops; D004789:Enzyme Activation; D007527:Isoenzymes / Q000378:metabolism*; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D015293:Transducin / Q000378:metabolism*
D007527:Isoenzymes; D010727:Phosphoric Diester Hydrolases; D015293:Transducin; D043265:Phosphatidylinositol Diacylglycerol-Lyase