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The cationic region of Rhes mediates its interactions with specific Gβ subunits

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Hill, Claire, Goddard, Alan, Ladds, Graham and Davey, John . (2009) The cationic region of Rhes mediates its interactions with specific Gβ subunits. Cellular Physiology and Biochemistry, Vol.23 (No.1-3). pp. 1-8. ISSN 1015-8987

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Official URL: http://dx.doi.org/10.1159/000204075

Abstract

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.

Item Type:	Journal Article
Subjects:	R Medicine > RB Pathology
Divisions:	Faculty of Medicine > Warwick Medical School > Clinical Sciences Research Institute (CSRI) Faculty of Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH):	Cationic proteins
Journal or Publication Title:	Cellular Physiology and Biochemistry
Publisher:	Karger
ISSN:	1015-8987
Date:	2009
Volume:	Vol.23
Number:	No.1-3
Number of Pages:	8
Page Range:	pp. 1-8
Identification Number:	10.1159/000204075
Status:	Peer Reviewed
Access rights to Published version:	Open Access
Funder:	Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Coventry and Warwickshire Hospitals Trust (CWHT)
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URI:	http://wrap.warwick.ac.uk/id/eprint/361