RGS18 (NMR): Human regulator of G-protein signalling 18
PDB Code: 2OWI
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. .
RGS 18 is a member of the B/R4 subfamily of RGS proteins, along with RGS1, RGS 2, RGS 3, RGS 4, RGS 5, RGS 13 and RGS 16. All of these subfamily members have an N-terminal amphipathic helix which enhances the localisation of the protein to the membrane surface where it is ideally placed to interact with the G-proteins.
RGS 18 expression is most abundant in megakaryocytes, platelets and monocytes is weakly expressed in hematopoietic stem cells. It binds to Gα i1, Gα i2, Gα i3, and Gα q but not Gα z, Gα s or Gα 12. Although no direct link to any specific disease is yet proven, RGS 18 is believed to play roles in the regulation of megakaryocyte differentiation, proliferation and chemotaxis, in platelet activation, and as an inhibitor for chemokine-induced dendritic cell migration. RGS 18 is believed to act primarily via inhibition of Gq signaling.
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