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Titolo:
Regulators of G protein signaling: A bestiary of modular protein binding domains
Autore:
Burchett, SA;
Indirizzi:
Yale Univ, Sch Med, Boyer Ctr Mol Med, Dept Pharmacol, New Haven, CT 06536USA Yale Univ New Haven CT USA 06536 , Dept Pharmacol, New Haven, CT 06536USA
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 4, volume: 75, anno: 2000,
pagine: 1335 - 1351
SICI:
0022-3042(200010)75:4<1335:ROGPSA>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; NUCLEOTIDE EXCHANGE FACTOR; METABOTROPIC GLUTAMATE RECEPTORS; MESSENGER-RNA EXPRESSION; BLOOD MONONUCLEAR-CELLS; ALPHA-FACTOR PHEROMONES; ACTIVITY IN-VITRO; RGS PROTEINS; SACCHAROMYCES-CEREVISIAE; PLASMA-MEMBRANE;
Keywords:
regulator of G protein signaling; polybasic domain; GGL domain; DEP domain; polyproline domain; Sst2;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
128
Recensione:
Indirizzi per estratti:
Indirizzo: Burchett, SA Yale Univ, Sch Med, Boyer Ctr Mol Med, Dept Pharmacol, 295 Congress Ave,Rm436, New Haven, CT 06536 USA Yale Univ 295 Congress Ave,Rm 436New Haven CT USA 06536 USA
Citazione:
S.A. Burchett, "Regulators of G protein signaling: A bestiary of modular protein binding domains", J NEUROCHEM, 75(4), 2000, pp. 1335-1351

Abstract

Members of the newly discovered regulator of G protein signaling (RGS) families of proteins have a common RGS domain. This RGS domain is necessary for conferring upon RGS proteins the capacity to regulate negatively a variety of G alpha protein subunits, However, RGS proteins are more than simply negative regulators of signaling. RGS proteins can function as effector antagonists, and recent evidence suggests that RGS proteins can have positive effects on signaling as well. Many RGS proteins possess additional C- and N-terminal modular protein-binding domains and motifs. The presence of these additional modules within the RGS proteins provides for multiple novel regulatory interactions performed by these molecules. These regions are involved in conferring regulatory selectivity to specific G alpha-coupled signaling pathways, enhancing the efficacy of the RGS domain, and the translocationor targeting of RGS proteins to intracellular membranes. In other instances, these domains are involved in cross-talk between different G alpha-coupled signaling pathways and, in some cases, likely serve to integrate small GTPases with these G protein signaling pathways. This review discusses theseC- and N-terminal domains and their roles in the biology of the brain-enriched RGS proteins. Methods that can be used to investigate the function of these domains are also discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/21 alle ore 05:23:34