Abstract
A-to-I pre-mRNA editing by adenosine deaminase enzymes has been reported to enhance protein diversity in the nervous system. In Drosophila, the resistance to dieldrin (RDL) gamma-aminobutyric acid (GABA) receptor subunit displays an editing site (R122) that is close to the putative GABA-binding site. We assessed the functional effects of editing at this site by expressing homomeric RDL receptors in Xenopus oocytes. After replacement of arginine 122 with a glycine, both agonist and fipronil potencies were shifted to the right in either fipronil-sensitive receptors or mutated resistant receptors (A301G/T350M). These data provide the first insight on the influence of RNA editing on GABA receptor function.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Arginine / genetics
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Dose-Response Relationship, Drug
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Drosophila
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Drosophila Proteins
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Gene Expression / drug effects*
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Insect Proteins / physiology*
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Insecticides / pharmacology*
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Membrane Potentials / drug effects
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Membrane Potentials / physiology
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Membrane Potentials / radiation effects
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Models, Molecular
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Mutation / physiology
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Oocytes
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Patch-Clamp Techniques
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Pyrazoles / pharmacology*
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RNA Editing / physiology*
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Receptors, GABA / genetics
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Receptors, GABA / physiology*
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Xenopus laevis
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gamma-Aminobutyric Acid / pharmacology
Substances
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Drosophila Proteins
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Insect Proteins
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Insecticides
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Pyrazoles
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Receptors, GABA
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gamma-Aminobutyric Acid
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Arginine
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fipronil