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Abstract
The regulators of heterotrimeric guanosine triphosphate (GTP)-binding protein (G protein) signaling (RGS proteins) were named for their ability to act as GTP-activating proteins (GAPs) for G proteins and, thus, limit the signal generated by G protein-coupled receptors (GPCRs). In addition to this characteristic biochemical trait, RGS proteins constitute a large family of structurally diverse proteins with variable sequence motifs that permit additional specific interactions. RGS proteins may also serve as a bridge from GPCRs to receptor tyrosine kinases or transmembrane channels, allowing signals from GPCRs to regulate signaling through other types of receptors, and vice versa.
