RGS17: Human regulator of G-protein signalling 17
PDB Code: 1ZV4
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.
RGS17 is a member of the A or Rz subfamily of regulators and has been shown to preferentially inhibit signalling through Gαi/o, Gαq and Gαs. This subfamily contains a cysteine rich region on their N-termini which is the interaction site for GAIP interacting protein. This protein is involved in the degradation of Gαi with an Rz RGS protein forming the linker between Gαi and GIPN.
Enriched expression of RGS17 is found in the brain. One of the clinically important roles that RGS17 plays in the brain is to regulate the activity of µ-opoid receptors. It has been shown that RGS17 forms a complex with the m-opoid receptor producing acute tolerance to morphine administration by sequestering the Gα subunits. Potentially, RGS17 is involved in carcinogenesis by chromosomal rearrangement, a process that results in gene fusion, as RGS17 was found to form a fusion with the IRA1 gene promotor in the breast cancer cell line MCF7.

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