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

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  Publication Details (including relevant citation   information): Ford,C.E., Skiba,N.P., Bae,H., Daaka,Y.,   Reuveny,E., Shekter,L.R., Rosal,R., Weng,G., Yang,C.S.,   Iyengar,R., Miller,R.J., Jan,L.Y., Lefkowitz,R.J., Hamm,H.E.,   Science, 1998, 280 (5367), pp   1271-1274

  Abstract: 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.

  Address (URL): http://www.hubmed.org/display.cgi?uids=9596582