Disease relevance of RGS8

• Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus [1].
• It describes three kinds of in vitro-binding experiments using RGS8 proteins generated by three different techniques: recombinant protein from Escherichia coli, in vitro-translated protein, and protein expressed in cDNA-transfected cultured cells [2].

High impact information on RGS8

• RGS8 does not directly interact with G-protein-coupled receptors [3].
• Furthermore, CCG-4986 is selective for RGS4 and does not inhibit RGS8 [4].
• Coexpression of full-length RGS3T, RGS3, or RGS8 significantly attenuated the magnitude of receptor-mediated Ca channel inhibition [5].
• Alternative splicing of RGS8 gene changes the binding property to the M1 muscarinic receptor to confer receptor type-specific Gq regulation [6].
• These results demonstrated that RGS8 is recruited to the plasma membrane where G-proteins are activated mainly by direct association with Galpha [7].

Biological context of RGS8

• Our results with the neuronal protein, RGS8, show that the enhancement of activation kinetics is a variable phenomenon determined by receptor type, G-protein isoform and RGS8 expression levels [8].

Anatomical context of RGS8

• Thus, it is evident that there is a novel mechanism controlling the distribution of RGS8 protein in cerebellar Purkinje cells [9].

Other interactions of RGS8

• Participation of RGS8 in the ternary complex of agonist, receptor and G-protein [8].
• Biochemical studies indicated that RGS8 binds to Galphao and Galphai3, and that it functions as a GTPase-activating protein (GAP) for Galpha subunits [9].

Analytical, diagnostic and therapeutic context of RGS8

• In situ hybridization analysis showed a highly dense expression of RGS8 mRNA in Purkinje cells of the cerebellum in rat brain [9].

References