TY - CHAP
T1 - The superfamily of "regulator of g-protein signaling" (rgs) proteins
AU - Willard, Melinda D.
AU - Willard, Francis S.
AU - Siderovski, David P.
N1 - Funding Information:
We thank Dr T. Kendall Harden (UNC-Chapel Hill) for contributions made to the first version of this chapter in 2003. Work on the RGS proteins in the Siderovski laboratory is supported in part by R01 grants GM062338 and GM074268 from the National Institute of General Medical Sciences, US Department of Health and Human Services.
Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
PY - 2010
Y1 - 2010
N2 - A large family of seven transmembrane-domain receptors for hormones, neurotransmitters, growth factors, chemoattractants, light, odorants, and other extracellular stimuli promote intracellular signaling responses by activation of heterotrimeric G proteins. This discrepancy between the rates of GTP hydrolysis measured in vitro and in vivo presaged the existence of proteins that accelerate the deactivation of GTP-bound Gα subunits. In the standard model of GPCR signaling, the duration of heterotrimeric G-protein signaling through effectors is thought to be controlled by the lifetime of the Gα subunit in its GTP-bound form. Regulator of G-protein Signaling (RGS) proteins promote the deactivation step in the heterotrimeric G-protein regulatory cycle, catalyzing GTPase rates in vitro that are consistent with the rates of deactivation of G-protein signaling in vivo. The physiological functions of these proteins continue to be investigated and, in the case of many RGS proteins, include additional functionalities beyond their hallmark capacity to act as GAPs for Gα subunits.
AB - A large family of seven transmembrane-domain receptors for hormones, neurotransmitters, growth factors, chemoattractants, light, odorants, and other extracellular stimuli promote intracellular signaling responses by activation of heterotrimeric G proteins. This discrepancy between the rates of GTP hydrolysis measured in vitro and in vivo presaged the existence of proteins that accelerate the deactivation of GTP-bound Gα subunits. In the standard model of GPCR signaling, the duration of heterotrimeric G-protein signaling through effectors is thought to be controlled by the lifetime of the Gα subunit in its GTP-bound form. Regulator of G-protein Signaling (RGS) proteins promote the deactivation step in the heterotrimeric G-protein regulatory cycle, catalyzing GTPase rates in vitro that are consistent with the rates of deactivation of G-protein signaling in vivo. The physiological functions of these proteins continue to be investigated and, in the case of many RGS proteins, include additional functionalities beyond their hallmark capacity to act as GAPs for Gα subunits.
UR - http://www.scopus.com/inward/record.url?scp=84882881043&partnerID=8YFLogxK
U2 - 10.1016/B978-0-12-374145-5.00206-0
DO - 10.1016/B978-0-12-374145-5.00206-0
M3 - Chapter
AN - SCOPUS:84882881043
SN - 9780123741455
VL - 2
SP - 1683
EP - 1703
BT - Handbook of Cell Signaling, 2/e
PB - Elsevier Inc.
ER -