A conserved aspartate determines pore properties of anion channels associated with excitatory amino acid transporter 4 (EAAT4).

@article{Kovermann2010ACA,
  title={A conserved aspartate determines pore properties of anion channels associated with excitatory amino acid transporter 4 (EAAT4).},
  author={Peter Kovermann and Jan-Philipp Machtens and David Ewers and Christoph Fahlke},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 31},
  pages={23676-86}
}
Excitatory amino acid transporter (EAAT) glutamate transporters function not only as secondary active glutamate transporters but also as anion channels. Recently, a conserved aspartic acid (Asp(112)) within the intracellular loop near to the end of transmembrane domain 2 was proposed as a major determinant of substrate-dependent gating of the anion channel associated with the glial glutamate transporter EAAT1. We studied the corresponding mutation (D117A) in another EAAT isoform, EAAT4, using… CONTINUE READING
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Modification of EAAT4 Anion Channel Gating

  • N. Melzer, A. Biela, Fahlke, Ch
  • J. Biol. Chem. 278,
  • 2003

Introduction to Membrane Noise (DeFelice, L

  • L. J. DeFelice
  • 1981

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