Regulator of G Protein Signaling 5 (RGS5)
Reference work entry
Regulator of G protein signaling (RGS) molecules comprise a large family of proteins (>35 in mammals) which modulate signaling downstream of G protein-coupled receptors (GPCRs). All family members share an evolutionary conserved RGS domain which confers guanosine triphosphatase (GTPase) activity (GAP) for the heterotrimeric G protein alpha subunit (Gα). Upon GPCR activation and Gα dissociation, RGS molecules facilitate GTP hydrolysis by the Gα subunit and thus accelerate reassociation of heterotrimeric G proteins with their receptors and termination of GPCR signaling. RGS molecules are therefore negative regulators of GPCR signaling (Fig. 1). RGS5 belongs to the B/R4 subfamily of RGS molecules and – like other B/R4 proteins such as RGS1, 2, 3, 4, 8, 13, 16, 18, and 21 – is a small protein with little more than a 120 aa RGS domain and 33 aa N-terminal part which is important for membrane association (Fig. 2a) (Ganss 2015...
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