2021•IUPHAR/BPS Guide to Pharmacology CITEOpen access
Regulators of G protein Signaling (RGS) proteins in GtoPdb v.2021.2
Katelin E. Ahlers‐Dannen, Mohammed Alqinyah, Christopher Bodle, Josephine Bou Dagher, Bandana Chakravarti, Shreoshi Pal Choudhuri, Kirk M. Druey, Rory Alan Fisher, Kyle J. Gerber, John R. Hepler, Shelley B. Hooks, Havish Sairaju Kantheti, Behirda Karaj, Somayeh Layeghi‐Ghalehsoukhteh, Jae‐Kyung Lee, Zili Luo, Kirill A. Martemyanov, Luke D. Mascarenhas, Harrison J. McNabb, Carolina Montañez‐Miranda, Osita W. Ogujiofor, Hoa T. N. Phan, David L. Roman, Vincent S. Shaw, Benita Sjögren, Mackenzie M. Spicer, Katherine E. Squires, Laurie P. Sutton, Menbere Wendimu, Thomas Martin Wilkie, Keqiang Xie, Qian Zhang, Yalda Zolghadri
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Abstract
Regulator of G protein Signaling, or RGS, proteins serve an important regulatory role in signaling mediated by G protein-coupled receptors (GPCRs). They all share a common RGS domain that directly interacts with active, GTP-bound Gα subunits of heterotrimeric G proteins. RGS proteins stabilize the transition state for GTP hydrolysis on Gα and thus induce a conformational change in the Gα subunit that accelerates GTP hydrolysis, thereby effectively turning off signaling cascades mediated by GPCRs. This GTPase accelerating protein (GAP) activity is the canonical mechanism of action for RGS proteins, although many also possess additional functions and domains. RGS proteins are divided into four families, R4, R7, R12 and RZ based on sequence homology, domain structure as well as specificity towards Gα subunits. For reviews on RGS proteins and their potential as therapeutic targets, see e.g. [225, 529, 578, 583, 584, 742, 753, 444, 10].
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