Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

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

Tools
- Tools
+ Tools

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. doi:10.1159/000204075 ISSN 1015-8987.

[img]
Preview
PDF
WRAP_Ladds_9576638-060109-Hill_et_al_2009_All.pdf - Requires a PDF viewer.

Download (558Kb)
Official URL: http://dx.doi.org/10.1159/000204075

Request Changes to record.

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 Science, Engineering and Medicine > 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
Official Date: 2009
Dates:
DateEvent
2009Published
Volume: Vol.23
Number: No.1-3
Number of Pages: 8
Page Range: pp. 1-8
DOI: 10.1159/000204075
Status: Peer Reviewed
Access rights to Published version: Open Access (Creative Commons)
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Coventry and Warwickshire Hospitals Trust (CWHT)

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us