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• W1966246128 abstract "The selective manipulation of single intracellular-signaling events remains one of the key tasks when studying signaling networks. Here, we demonstrate for the first time the stimulation of FKBP fusions of various subunits of heterotrimeric G proteins by the simple addition of the chemical dimerizer rapamycin. Activation of constitutively active Gαq, but not its GDP-bound form, leads to sustained oscillations of intracellular calcium and myo-inositol 1,4,5-trisphosphate (InsP3) levels in HEK cells, independent of the activation of endogenous Gαq, in full agreement with the InsP3-Ca2+ cross-coupling model of calcium oscillations. Rapamycin-induced translocation of wild-type Gαs to the plasma membrane results in elevated cAMP levels. Activation of rapamycin-inducible Gαs or Gβ1γ2 evokes extensive modulation of ATP-induced calcium transients. The results demonstrate that inducible heterotrimeric G protein subunits will provide ways for dissecting G protein-coupled receptor signaling." @default.
• W1966246128 created "2016-06-24" @default.
• W1966246128 creator A5028191617 @default.
• W1966246128 creator A5069111179 @default.
• W1966246128 date "2011-09-01" @default.
• W1966246128 modified "2023-10-18" @default.
• W1966246128 title "Switching Heterotrimeric G Protein Subunits with a Chemical Dimerizer" @default.
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• W1966246128 doi "https://doi.org/10.1016/j.chembiol.2011.07.013" @default.
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