GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins.

Content Provider	Semantic Scholar
Author	Ross, Elliott M. Wilkie, Thomas M.
Copyright Year	2000
Abstract	GTPase-activating proteins (GAPs) regulate heterotrimeric G proteins by increasing the rates at which their subunits hydrolyze bound GTP and thus return to the inactive state. G protein GAPs act allosterically on G subunits, in contrast to GAPs for the Ras-like monomeric GTP-binding proteins. Although they do not contribute directly to the chemistry of GTP hydrolysis, G protein GAPs can accelerate hydrolysis >2000-fold. G protein GAPs include both effector proteins (phospholipase C-¿, p115RhoGEF) and a growing family of regulators of G protein signaling (RGS proteins) that are found throughout the animal and fungal kingdoms. GAP activity can sharpen the termination of a signal upon removal of stimulus, attenuate a signal either as a feedback inhibitor or in response to a second input, promote regulatory association of other proteins, or redirect signaling within a G protein signaling network. GAPs are regulated by various controls of their cellular concentrations, by complex interactions with G¿ or with G¿5 through an endogenous G-like domain, and by interaction with multiple other proteins.
Starting Page	795
Ending Page	827
Page Count	33
File Format	PDF HTM / HTML
DOI	10.1146/annurev.biochem.69.1.795
Alternate Webpage(s)	http://www4.utsouthwestern.edu/rosslab/PDF_files/Ross%202000%20AnnuRev.pdf
PubMed reference number	10966476
Alternate Webpage(s)	https://doi.org/10.1146/annurev.biochem.69.1.795
Journal	Medline
Volume Number	69
Journal	Annual review of biochemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article