RGS14 (NMR): Human regulator of G-protein signalling 14
PDB Code: 2JNU
Regulators of G-protein signalling (RGS) are domains that terminate the signal emanating from G-protein coupled receptors (GPCR). When a GPCR binds a specific ligand, a signal is generated that is transmitted to the G-proteins that consist of the Gα and Gβγ subunits. In the inactive state Gα and Gβγ exist as a complex with the Gα GTPase in an inactive GDP bound state. Upon activation GDP is replaced with GTP which induces Gα and Gβγ complex disassociation. At this stage both Gα and Gβγ proteins are active. Gα does have an intrinsic GTPase activity but this is greatly enhanced by the association with an RGS domain. Hence RGS proteins act as GTPase activating proteins (GAPs). Once GTP hydrolysis has taken place the GDP-Gα protein can recombine with Gβγ thus terminating the signal. .
RGS14 is a member of the D/R12 subfamily of RGS proteins. RGS14 comprises an RGS domain that confers GAP activity for the Go/iα subfamily of G proteins, a central tandem RBDs (Raf-like Ras/Rap binding domains) that binds the GTPases, Rap1 and Rap2 and a GoLoco or G-protein regulatory motif that acts as a GDI (guanine nucleotide dissociation inhibitor) for Giα1 and Giα3. RGS14 stimulates the GTPase activity of Gαi and Gαo in vitro and down-regulates signalling from GPCRs acting through Gi. The RGS and GoLoco domains of RGS14 are independently able to inhibit downstream signalling of Gi but they also cooperate to maximally down-regulate Gi pathways. RGS14 is expressed in the brain, lung and spleen and has been shown to attenuate IL-8 receptor-mediated MAP kinase activation and M1 acetylcholine receptor-stimulated c-fos SRE activation.
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