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J Comp Neurol. 2011 Oct 1;519(14):2734-57. doi: 10.1002/cne.22649.

Involvement of the Drosophila taurine/aspartate transporter dEAAT2 in selective olfactory and gustatory perceptions.

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  • 1Developmental Biology Institute of Marseille (IBDML), Centre National de la Recherche Scientifique (CNRS) UMR 6216, Université Aix-Marseille II-III, 13288 Marseille cedex 9, France. marie-therese.besson@univmed.fr

Abstract

Excitatory amino acid transporters (EAATs) are membrane proteins involved in the uptake of neurotransmitter amino acids in the nervous system. The Drosophila dEAAT2 gene was previously described to encode a taurine/aspartate transporter. To analyze further the expression pattern and physiological function of this protein, we generated transgenic flies containing either the dEAAT2 promoter region fused to GAL4 (dEAAT2-GAL4) or a transgene allowing expression of a dEAAT2::GFP fusion protein (UAS-dEAAT2::GFP). We observed that dEAAT2-GAL4 expresses green fluorescent protein (GFP) in neurons in central and peripheral structures of third-instar larvae and adult flies. Labeled neurons were found in olfactory and gustatory pathways, in which dEAAT2::GFP was detected from the dendrites of the sensory neurons up to the first- and second-order centers. dEAAT2-GAL4 is also expressed in mechanosensory neurons. We found that a viable piggyBac insertion strain disrupts dEAAT2 expression. This mutant appears morphologically normal and presents no locomotor or phototaxis impairments; however, its brain taurine level is significantly reduced compared with that of wild-type flies. The dEAAT2 mutant showed decreased avoidance behavior in the presence of high concentration of propionic acid compared with wild-type flies, but no modification of the avoidance response to benzaldehyde. In gustatory tests, both mutant and control flies were normally attracted to sucrose; however, the dEAAT2 mutant presented a higher salt sensitivity, being repulsed by low and high salt concentrations. Therefore, we conclude that dEAAT2 does function as a taurine transporter in vivo and that this protein is physiologically required for the sensory perception of specific environmental molecules.

PMID:
21484805
DOI:
10.1002/cne.22649
[PubMed - indexed for MEDLINE]
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