Bridging with GAPs: receptor communication through RGS proteins.
The regulators of heterotrimeric guanosine triphosphate (GTP)-binding protein (G protein) signaling (RGS proteins) were named for their ability to act as GTP-activating proteins (GAPs) for G proteins and, thus, limit the signal generated by G protein-coupled receptors (GPCRs). In addition to this characteristic biochemical trait, RGS proteins constitute a large family of structurally diverse proteins with variable sequence motifs that permit additional specific interactions. RGS proteins may also serve as a bridge from GPCRs to receptor tyrosine kinases or transmembrane channels, allowing signals from GPCRs to regulate signaling through other types of receptors, and vice versa.
Druey
K M
KM
Molecular Signal Transduction Section, Laboratory of Allergic Diseases, National Institute of Allergy and Infectious Diseases/NIH, Rockville, MD 20852, USA. kdruey@nih.gov
D000818:Animals; D015220:Calcium Channels / Q000378:metabolism; D020690:GTPase-Activating Proteins / Q000737:chemistry / Q000502:physiology; D020962:Heterotrimeric GTP-Binding Proteins / Q000378:metabolism; D046911:Macromolecular Substances; D008954:Models, Biological; D017434:Protein Structure, Tertiary; D020710:RGS Proteins / Q000737:chemistry / Q000502:physiology*; D011956:Receptors, Cell Surface / Q000378:metabolism; D015398:Signal Transduction
D015220:Calcium Channels; D020690:GTPase-Activating Proteins; D046911:Macromolecular Substances; D020710:RGS Proteins; D011956:Receptors, Cell Surface; D020962:Heterotrimeric GTP-Binding Proteins