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The Cationic Region of Rhes Mediates its Interactions with Specific Gβ SubunitsHill C.3,* · Goddard A.1,* · Ladds G.2,# · Davey J.3,#
1Department of Biochemistry, University of Oxford,2Division of Clinical Sciences, Warwick Medical School3Department of Biological Sciences, University of Warwick, Coventry*These authors contributed equally to the work#These authors contributed equally to the work Corresponding Author
Dr Graham Ladds
Division of Clinical Sciences, Warwick Medical School
University of Warwick, Coventry, CV4 7AL (Great Britian)
Tel. +44 02476 528361, E-Mail Graham.Ladds@Warwick.ac.uk
Ras homologue enriched in striatum (Rhes) is a small monomeric G protein which functions in a variety of cellular processes, including attenuation of G protein-coupled receptor (GPCR) signalling. There have been many studies into the effects of Rhes, but there is no molecular information about how Rhes might bring about these effects. Rhes shares striking sequence homology to AGS1 (activator of G protein signalling 1) and we considered whether the two proteins function in similar ways. AGS1 binds to the Gβ1 subunit of heterotrimeric G proteins and we have used yeast two-hybrid studies to show that Rhes binds selectively to Gβ1, Gβ2 and Gβ3 subunits. Binding to the Gβ subunits involves the cationic regions of AGS1 and Rhes, and we used Rhes-AGS1 chimeras to show that their different cationic regions determine the Gβ-specificity of the interactions. Possible implications of this interaction for the activity of Rhes are discussed.
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