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• W2010357110 endingPage "359" @default.
• W2010357110 startingPage "352" @default.
• W2010357110 abstract "To study behavior of activated G(alpha)(s) in living cells, green fluorescent protein (GFP) was inserted within the internal amino acid sequence of G(alpha)(s) to generate a G(alpha)(s)-GFP fusion protein. The fusion protein maintained a bright green fluorescence and was identified by immunoblotting with antibodies against G(alpha)(s) or GFP. The cellular distribution of G(alpha)(s)-GFP was similar to that of endogenous G(alpha)(s). G(alpha)(s)-GFP was tightly coupled to the beta adrenergic receptor to activate the G(alpha)(s) effector, adenylyl cyclase. Activation of G(alpha)(s)-GFP by cholera toxin caused a gradual displacement of the fusion protein from the plasma membrane throughout the cytoplasm in living cells. Unlike the slow release of G(alpha)(s)-GFP from the membrane induced by cholera toxin, the beta-adrenergic agonist isoproterenol caused a rapid partial release of the fusion protein into the cytoplasm. At 1 min after treatment with isoproterenol, the extent of G(alpha)(s)-GFP release from plasma membrane sites was maximal; however, insertion of G(alpha)(s)-GFP at other membrane sites occurred during the same time period. Translocation of G(alpha)(s)-GFP fusion protein induced by isoproterenol suggested that the internalization of G(alpha)(s) might play a role in signal transduction by interacting with effector molecules and cytoskeletal elements at multiple cellular sites." @default.
• W2010357110 created "2016-06-24" @default.
• W2010357110 creator A5026181487 @default.
• W2010357110 creator A5036010034 @default.
• W2010357110 date "2002-02-01" @default.
• W2010357110 modified "2023-10-17" @default.
• W2010357110 title "Real-Time Visualization of a Fluorescent Gα_s: Dissociation of the Activated G Protein from Plasma Membrane" @default.
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• W2010357110 doi "https://doi.org/10.1124/mol.61.2.352" @default.
• W2010357110 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11809860" @default.
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