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Sci. STKE, 16 October 2001
Vol. 2001, Issue 104, p. re14
[DOI: 10.1126/stke.2001.104.re14]

REVIEWS

Bridging with GAPs: Receptor Communication Through RGS Proteins

Kirk M. Druey

Molecular Signal Transduction Section, Laboratory of Allergic Diseases, National Institute of Allergy and Infectious Diseases/NIH, Rockville, MD 20852 USA.

Contact information: Tel.: 301-435-8875, Fax: 301-402-7271, E-mail: kdruey{at}nih.gov

Numerous hormones and neurotransmitters send intracellular signals through receptors that have a heptahelical structure and are linked to heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins). G proteins consist of a complex of {alpha}, ß, and {gamma} subunits, and transmission of the signal depends on receptor-stimulated guanosine diphosphate (GDP)-GTP exchange by the {alpha} subunit. G{alpha} terminates signaling by hydrolyzing GTP to GDP. Regulators of G protein signaling (RGS proteins) inhibit signal transduction by enhancing the rate of G{alpha} GTP hydrolysis. RGS proteins comprise a large, heterogeneous family characterized by diverse sequence motifs, in addition to an "RGS box" that confers their signature enzymatic activity. This review discusses some of the other domains in RGS proteins and their newly appreciated role in linking assorted cell surface receptors to G protein signaling.

Citation:
K. M. Druey, Bridging with GAPs: Receptor Communication Through RGS Proteins. Science's STKE (2001), http://stke.sciencemag.org/cgi/content/full/OC_sigtrans;2001/104/re14.

© 2001 American Association for the Advancement of Science

Citation: K. M. Druey, Bridging with GAPs: Receptor Communication Through RGS Proteins. Sci. STKE 2001, re14 (2001).

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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)