Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Career Basics

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 23 February 1996:
Vol. 271. no. 5252, pp. 1056 - 1058
DOI: 10.1126/science.271.5252.1056
Prev | Table of Contents | Next

Research News

Wade Roush

Cell biologists have long known that cells can damp down their responses to hormones, neurotransmitters, and other regulators, but exactly how this "desensitization" occurs has been unclear. Now a flurry of work from several labs is revealing how one major group of intracellular communication lines--those using G proteins to transmit signals to the cell interior--achieves this volume control. Researchers have identified a new family of proteins, known as the RGS proteins (for regulators of G protein signaling), that attenuate signaling through those pathways, apparently by binding to one of the three protein subunits that make up a complete G protein. The new findings could lead to a much better understanding of how G protein-signal pathways work--information that could have practical implications as up to 60% of all drugs exert their effects through these pathways.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Control of the Expression and Activity of the Galpha -interacting Protein (GAIP) in Human Intestinal Cells.
E. Ogier-Denis, A. Petiot, C. Bauvy, and P. Codogno (1997)
J. Biol. Chem. 272, 24599-24603
   Abstract »    Full Text »    PDF »
The Retinal Specific Protein RGS-r Competes with the gamma Subunit of cGMP Phosphodiesterase for the alpha Subunit of Transducin and Facilitates Signal Termination.
T. Wieland, C.-K. Chen, and M. I. Simon (1997)
J. Biol. Chem. 272, 8853-8856
   Abstract »    Full Text »    PDF »
The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro.
E. Faurobert and J. B. Hurley (1997)
PNAS 94, 2945-2950
   Abstract »    Full Text »    PDF »
Characterization of a Novel Mammalian RGS Protein That Binds to Galpha Proteins and Inhibits Pheromone Signaling in Yeast.
C. Chen, B. Zheng, J. Han, and S.-C. Lin (1997)
J. Biol. Chem. 272, 8679-8685
   Abstract »    Full Text »    PDF »
GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Galpha i subunits.
L. De Vries, E. Elenko, L. Hubler, T. L. Z. Jones, and M. G. Farquhar (1996)
PNAS 93, 15203-15208
   Abstract »    Full Text »    PDF »
RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling.
C.-K. Chen, T. Wieland, and M. I. Simon (1996)
PNAS 93, 12885-12889
   Abstract »    Full Text »    PDF »
The GTPase-activating Protein RGS4 Stabilizes the Transition State for Nucleotide Hydrolysis.
D. M. Berman, T. Kozasa, and A. G. Gilman (1996)
J. Biol. Chem. 271, 27209-27212
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)