Bridging with GAPs: Receptor Communication Through RGS Proteins

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Science's STKE  16 Oct 2001:
Vol. 2001, Issue 104, pp. re14
DOI: 10.1126/stke.2001.104.re14

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Numerous hormones and neurotransmitters send intracellular signals through receptors that have a heptahelical structure and are linked to heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins). G proteins consist of a complex of α, β, and γ subunits, and transmission of the signal depends on receptor-stimulated guanosine diphosphate (GDP)-GTP exchange by the α subunit. Gα terminates signaling by hydrolyzing GTP to GDP. Regulators of G protein signaling (RGS proteins) inhibit signal transduction by enhancing the rate of Gα GTP hydrolysis. RGS proteins comprise a large, heterogeneous family characterized by diverse sequence motifs, in addition to an "RGS box" that confers their signature enzymatic activity. This review discusses some of the other domains in RGS proteins and their newly appreciated role in linking assorted cell surface receptors to G protein signaling.