RGS3: Human regulator of G-protein signalling 3, PDZ domain
PDB Code: 2F5Y
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 G bg thus terminating the signal.
RGS 3 is a member of the B/R4 subfamily of RGS proteins. However, unlike the other sub-family members RGS 3 has a long N-terminal section that contains a PDZ domain. In general, PDZ domains bind to specific C-termini of their target proteins. The PDZ domain of RGS 3 has been shown to interact with the C-terminus of Ephrin-B, proteins involved in contact dependent cell-to-cell communication and signal transmission. When the RGS 3 PDZ domain binds to Ephrin-B the RGS domain of RGS 3 blocks the signal from the activated CXCR4 GPCR. At birth, granule cells are prevented from circulating through this activation of the CXCR4 receptor with the RGS 3-mediated block of the CXCR4 signal initiating cell migration for the new born.
Cell migration is clearly a key mechanism in the spread of tumors. Highly migratory glioblastoma cells were analysed for differential gene expression with both RGS 3 and RGS 4 being upregulated. Cells over-expressing these genes demonstrated an increase in cell adhesion and migration. These results hint at the possibility of RGS proteins playing a pivotal role in the control of cell mobility.
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