Hormone signalling via G-protein: regulation of phosphatidylinositol 4,5-bisphosphate hydrolysis by G q

Abstract

Heterotrimeric GTP-dependent regulatory proteins (G-proteins) mediate modulation by many cell surface receptors. Activation of the G-proteins promotes dissociation of their α and βγ subunits. The similarity of behaviour of βγ subunits derived from a variety of G-proteins has led to their use as affinity reagents for the analysis of the more unique a subunits. The evolution of these uses is presented. One of the more insightful results was the isolation of a new class of G -protein α subunits (the α q subfamily) which have been shown to regulate the activity of a phospholipase C (PLC) specific for phosphatidylinositols. The experimental evidence leading to this conclusion is discussed. The activation by α q increases the apparent V max of the β isoform of phosphatidylinositol-specific phospholipase C (PLCβ) and can be modulated by βγ subunits.