RGS10 is a selective activator of G alpha i GTPase activity.

Polypeptides that define a protein family termed RGS (for regulators of G-protein signalling) are encoded by the SST2 gene of the yeast Saccharomyces cerevisiae, the EGL-10 gene of the nematode Caenorhabdatis elegans, and several related mammalian genes. Genetic studies in invertebrates and mammalian cell-transfection experiments indicate that RGS proteins negatively ...
regulate signalling pathways involving seven transmembrane receptors and heterotrimeric G proteins. However, the biochemical mechanism by which RGS proteins control these pathways is unknown. Here we report the characterization of human RGS10, a member of this protein family. Co-immunoprecipitation studies demonstrate that RGS10 associates specifically with the activated forms of two related G-protein subunits, G alphai3, and G alphaz, but fails to interact with the structurally and functionally distinct G alphas subunit. In vitro assays with purified proteins indicate that RGS10 increases potently and selectively the GTP hydrolytic activity of several members of the G alphai family, including G alphai3, G alphaz, and G alpha0. These results demonstrate that RGS proteins can attenuate signalling pathways involving heterotrimeric G proteins by serving as GTPase-activating proteins for specific types of G alpha subunits.
Mesh Terms:
Amino Acid Sequence, Animals, Cloning, Molecular, Enzyme Activation, GTP Phosphohydrolases, GTP-Binding Proteins, Guanosine Triphosphate, Hela Cells, Humans, Hydrolysis, Molecular Sequence Data, Precipitin Tests, Proteins, RGS Proteins, Rats, Sequence Homology, Amino Acid, Signal Transduction
Nature
Date: Sep. 12, 1996
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