Specific in vivo binding of activator of G protein signalling 1 to the Gbeta1 subunit.
Activator of G protein signalling 1 ( AGS1) is a Ras-like protein that affects signalling through heterotrimeric G proteins. Previous in vitro studies suggest that AGS1 can bind to G(alpha)-GDP subunits and promote nucleotide exchange, leading to activation of intracellular signalling pathways. This model is consistent with in vivo evidence demonstrating that AGS1 activates both G(alpha)- and G(betagamma)-dependent pathways in the absence of ligand. However, it does not easily explain how AGS1 blocks G(betagamma)-dependent, but not G(alpha)-dependent, signalling following receptor activation. We have used yeast two hybrid analysis and co-immunoprecipitation studies in mammalian cells to demonstrate a direct interaction between AGS1 and the G(beta1) subunit of heterotrimeric G proteins. The interaction is specific for G(beta1) and involves the cationic region of AGS1 and the C-terminal region of G(beta1). Possible implications of this novel interaction for the activity of AGS1 are discussed.[1]References
- Specific in vivo binding of activator of G protein signalling 1 to the Gbeta1 subunit. Hiskens, R., Vatish, M., Hill, C., Davey, J., Ladds, G. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
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