Molecular cloning and expression of the rat EAAT4 glutamate transporter subtype

Chien Liang Glenn Lin, Anastassios V. Tzingounis, Lin Jin, Akiko Furuta, Michael P. Kavanaugh, Jeffrey D. Rothstein

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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.

Original languageEnglish
Pages (from-to)174-179
Number of pages6
JournalMolecular Brain Research
Issue number1
StatePublished - Dec 10 1998


  • Cerebellum
  • Glutamate transporter
  • Ligand-gated chloride channel
  • Purkinje cell
  • cDNA


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