Guanine nucleotide binding regulatory proteins: Their characteristics and identification

Many biological signals are processed by the binding of chemicals to cell surface receptors. Signals are switched to intracellular language via guanine nucleotide binding regulatory proteins (G-proteins) which are present in all eukaryotic cells. Thus, G-proteins serve as interfaces between receptor-response coupling. Two forms of G-proteins have been reported: conventional G-proteins which are heterotrimeric and consist of α, β, and γ subunits, and monomeric small molecular weight G-proteins which are generally found as single polypeptides. Recently, high molecular weight G-proteins have also been described. The family of G-proteins contains multiple genes that encode the α, β, or γ subunits. G-proteins play a pivotal role in excitation-contraction coupling in smooth muscle function and control metabolic and secretory processes. In this review article, we have given a brief overview on the characteristics and methodology for the identification of G-proteins. The heterotrimeric G-proteins are generally identified by Western blotting and ADP-ribosylation with bacterial toxins. The monomeric and high molecular weight G-proteins have been identified by [³⁵S]GTPδS overlay technique and photoaffinity labeling, respectively. Recently, the use of molecular genetic probes has made it possible to investigate the expression of the message for various G-proteins.