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XB-ART-13871
Brain Res Mol Brain Res 1998 Dec 10;631:174-9. doi: 10.1016/s0169-328x(98)00256-3.
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Molecular cloning and expression of the rat EAAT4 glutamate transporter subtype.

Lin CL , Tzingounis AV , Jin L , Furuta A , Kavanaugh MP , Rothstein JD .


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Glutamate transport is a primary mechanism for the synaptic inactivation of glutamate. Excitatory amino acid transporter 4 (EAAT4) is a novel glutamate transporter with properties of a ligand-gated chloride channel that was recently cloned from human brain. Here we report the cloning of rat EAAT4 (rEAAT4) cDNA from rat cerebellum. The nucleotide sequence of rEAAT4 was 88% identical to the human sequence, and the predicted peptide was 89% identical to the human protein. The transport activity encoded by rEAAT4 has high affinity for L-glutamate. In Xenopus laevis oocytes expressing rEAAT4, L-glutamate and other transporter substrates elicited a current predominantly carried by chloride ions. Like human EAAT4, the rEAAT4 mRNA was largely restricted to cerebellar Purkinje cells; the rEAAT4 protein was localized to Purkinje cell somas and dendrites.

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Species referenced: Xenopus laevis
Genes referenced: slc1a6