ISSN:
1432-1912
Keywords:
Key words Heterotrimeric G proteins
;
GTPase-activating proteins
;
RGS proteins
;
Recovery
;
Desensitization
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract In a variety of signalling pathways heterotrimeric guanine-nucleotide-binding proteins (G proteins) trigger physiological responses elicited by hormones, neurotransmitters and sensory stimuli. Receptor-induced GDP/ GTP exchange activates G proteins by dissociating G-protein α-subunits from the βγ-dimers. Both α-subunits and βγ-dimers are involved in effector regulation. The deactivation of these active forms is controlled by the hydrolysis of GTP bound to α-subunits, allowing the inactive heterotrimer to reform. Termination of G-protein-mediated signalling in vivo is 10- to 100-fold faster than the in vitro rate of GTP hydrolysis by α-subunits, suggesting that in analogy to the GTPases of the Ras-superfamily, GTPase-activating proteins (GAPs) are required to achieve timely deactivation. Recently, members of a novel protein superfamily, known as “regulators of G-protein signalling” (RGS), were identified as potent GAPs for at least one subset of heterotrimeric G-protein α-subunits. In this review, we intend to discuss the proposed mechanism by which RGS proteins exert GAP activity for G-protein α-subunits as well as their specificities. The role of RGS proteins in desensitization and temporal resolution in certain signalling pathways will also be addressed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002109900031
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