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

Claire Hill, Alan Goddard, Graham Ladds*, John Davey

*Corresponding author for this work

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalCellular Physiology and Biochemistry
Volume23
Issue number1-3
DOIs
Publication statusPublished - Feb 2009

Bibliographical note

© 2009 S. Karger AG, Basel. Creative Commons Attribution Non-Commercial No Derivatives License 4.0 International

Keywords

  • AGS1
  • cationic region
  • Gβ subunit
  • Rhes

Fingerprint Dive into the research topics of 'The cationic region of Rhes mediates its interactions with specific Gβ subunits'. Together they form a unique fingerprint.

  • Cite this