Regulators of G protein Signaling (RGS) proteins (version 2020.5) in the IUPHAR/BPS Guide to Pharmacology Database

  • Katelin E. Ahlers-Dannen University of Iowa
  • Mohammed Alqinyah University of Georgia
  • Christopher Bodle University of Iowa
  • Josephine Bou Dagher University of Georgia
  • Bandana Chakravarti University of Iowa
  • Shreoshi P. Choudhuri University of Texas Southwestern Medical Center
  • Kirk M. Druey National Institutes of Health
  • Rory A. Fisher University of Iowa
  • Kyle J. Gerber Emory University
  • John R. Hepler Emory University
  • Shelley B. Hooks University of Georgia
  • Havish S. Kantheti University of Texas Southwestern Medical Center
  • Behirda Karaj Michigan State University
  • Jae-Kyung Lee University of Georgia
  • Zili Luo University of Iowa
  • Kirill Martemyanov Scripps Research Institute
  • Luke D. Mascarenhas University of Texas Southwestern Medical Center
  • Carolina Montañez-Miranda Emory University School of Medicine
  • Hoa Phan Thi Nhu Michigan State University
  • David L. Roman University of Iowa
  • Vincent Shaw Michigan State University
  • Benita Sjögren Purdue University
  • Mackenzie M. Spicer University of Iowa
  • Katherine E. Squires Emory University
  • Laurie Sutton Scripps Research Institute
  • Menbere Wendimu University of Georgia
  • Thomas M. Wilkie University of Texas Southwestern Medical Center
  • Keqiang Xie Scripps Research Institute
  • Yalda Zolghadri University of Texas Southwestern Medical Center


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. [183, 411, 446, 450, 451, 558, 566, 345, 9].

How to Cite
Ahlers-Dannen, K. E., Alqinyah, M., Bodle, C., Bou Dagher, J., Chakravarti, B., Choudhuri, S. P., Druey, K. M., Fisher, R. A., Gerber, K. J., Hepler, J. R., Hooks, S. B., Kantheti, H. S., Karaj, B., Lee, J.-K., Luo, Z., Martemyanov, K., Mascarenhas, L. D., Montañez-Miranda, C., Phan Thi Nhu, H., Roman, D. L., Shaw, V., Sjögren, B., Spicer, M. M., Squires, K. E., Sutton, L., Wendimu, M., Wilkie, T. M., Xie, K. and Zolghadri, Y. (2020) “Regulators of G protein Signaling (RGS) proteins (version 2020.5) in the IUPHAR/BPS Guide to Pharmacology Database”, IUPHAR/BPS Guide to Pharmacology CITE, 2020(5). doi: 10.2218/gtopdb/F891/2020.5.