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Publication : In situ assay of light-stimulated G protein activity in Drosophila photoreceptor G protein beta mutants.

First Author  Yarfitz S L Year  1994
Journal  J Biol Chem Volume  269
Pages  30340-4 PubMed ID  7982946
Abstract Text  An in situ 35S-labeled guanosine 5'-3-O-(thio)triphosphate (GTP gamma S) binding procedure was developed to assay light-stimulated G protein activity in Drosophila compound eyes. We found that Drosophila with mutations in G beta e, an abundant photoreceptor-specific G protein beta subunit essential for photoexcitation, are defective in light-stimulated [35S]GTP gamma S binding. We confirmed that G beta e interacts with a GTP-binding protein by demonstrating that immunoprecipitation of G beta e is sensitive to GTP gamma S. These results suggest that G beta e functions as the beta subunit of a heterotrimeric G protein that couples photoactivation of rhodopsin to downstream components in the Drosophila phototransduction cascade. Issue  48
Month  Dec

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