Molecular basis for interactions of G protein betagamma subunits with effectors.

Journal Article (Journal Article)

Both the alpha and betagamma subunits of heterotrimeric guanine nucleotide-binding proteins (G proteins) communicate signals from receptors to effectors. Gbetagamma subunits can regulate a diverse array of effectors, including ion channels and enzymes. Galpha subunits bound to guanine diphosphate (Galpha-GDP) inhibit signal transduction through Gbetagamma subunits, suggesting a common interface on Gbetagamma subunits for Galpha binding and effector interaction. The molecular basis for interaction of Gbetagamma with effectors was characterized by mutational analysis of Gbeta residues that make contact with Galpha-GDP. Analysis of the ability of these mutants to regulate the activity of calcium and potassium channels, adenylyl cyclase 2, phospholipase C-beta2, and beta-adrenergic receptor kinase revealed the Gbeta residues required for activation of each effector and provides evidence for partially overlapping domains on Gbeta for regulation of these effectors. This organization of interaction regions on Gbeta for different effectors and Galpha explains why subunit dissociation is crucial for signal transmission through Gbetagamma subunits.

Full Text

Duke Authors

Cited Authors

  • Ford, CE; Skiba, NP; Bae, H; Daaka, Y; Reuveny, E; Shekter, LR; Rosal, R; Weng, G; Yang, CS; Iyengar, R; Miller, RJ; Jan, LY; Lefkowitz, RJ; Hamm, HE

Published Date

  • May 22, 1998

Published In

Volume / Issue

  • 280 / 5367

Start / End Page

  • 1271 - 1274

PubMed ID

  • 9596582

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.280.5367.1271


  • eng

Conference Location

  • United States