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• W2039576559 endingPage "992" @default.
• W2039576559 startingPage "983" @default.
• W2039576559 abstract "Abstract: The neuronal protein GAP-43 is concentrated at the growth cone membrane, where it is thought to amplify the signal transduction process. As a model for its neuronal effects, GAP-43 protein injection into Xenopus laevis oocytes strongly augments the calcium-sensitive chloride current evoked by the G protein-coupled receptor stimulation. We have now examined a series of GAP-43 mutants in this system and determined those regions of GAP-43 required for this increase in current flux. As expected, palmitoylation inhibits signal amplification in oocytes by blocking G protein activation. Unexpectedly, a second domain of GAP-43 (residues 35–50) containing a protein kinase C phosphorylation site at residue 41 is also necessary for augmentation of G protein-coupled signals in oocytes. This region is not required for activation of isolated Go but is necessary for GAP-43 binding to isolated calmodulin and to isolated protein kinase C. Substitution of Asp for Ser41 inactivates GAP-43 as a signal facilitator in oocytes. This mutation blocks GAP-43 binding to both protein kinase C and calmodulin. Thus, GAP-43 regulates an oocyte signaling cascade via coordinated, simultaneous G protein activation and interaction with either calmodulin or protein kinase C." @default.
• W2039576559 created "2016-06-24" @default.
• W2039576559 creator A5014712166 @default.
• W2039576559 creator A5040964897 @default.
• W2039576559 creator A5074016785 @default.
• W2039576559 date "2002-11-14" @default.
• W2039576559 modified "2023-09-27" @default.
• W2039576559 title "GAP-43 Augmentation of G Protein-Mediated Signal Transduction Is Regulated by Both Phosphorylation and Palmitoylation" @default.
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• W2039576559 doi "https://doi.org/10.1046/j.1471-4159.1998.70030983.x" @default.
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