Background：

Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active， GTP-bound state and an inactive， GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP， thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:8774883， PubMed:18434541， PubMed:19478087). Signaling is mediated via effector proteins， such as adenylate cyclase. Inhibits adenylate cyclase activity， leading to decreased intracellular cAMP levels (PubMed:19478087). Stimulates the activity of receptor-regulated K+ channels (PubMed:2535845). The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the