Abstract

Both the α- and βγ-subunits of heterotrimeric guanine nucleotide-dependent regulatory proteins (G-proteins) couple members of the heptahelical class of cell-surface receptors to a diverse range of signal-generating effectors including retinal cyclic GMP phosphodiesterase, ion channels, adenylylcyclases, phosphoinositide 3-kinase, and members of the β-class of inositol lipid-specific phospholipases C. Although the molecular details of the G-protein-regulated phospholipase C system were elucidated comparatively recently, these enzymes have become an important model for investigations of the process of G-protein effector coupling. A combination of molecular biological, biochemical, and structural studies using the phospholipase C-β enzymes has provided some important insights into the interplay between G-proteins and their effectors and promises to reveal the mechanisms by which G-protein α- and βγ-subunits selectively associate with and activate effectors.

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