Authors: Christoph Fahlke Daniel Kortzak JanPhilipp Machtens
Publish Date: 2015/12/19
Volume: 468, Issue: 3, Pages: 491-502
Abstract
Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system After release from presynaptic nerve terminals glutamate is quickly removed from the synaptic cleft by a family of five glutamate transporters the socalled excitatory amino acid transporters EAAT1–5 EAATs are prototypic members of the growing number of dualfunction transport proteins they are not only glutamate transporters but also anion channels Whereas the mechanisms underlying secondary active glutamate transport are well understood at the functional and at the structural level mechanisms and cellular roles of EAAT anion conduction have remained elusive for many years Recently molecular dynamics simulations combined with simulationguided mutagenesis and experimental analysis identified a novel anionconducting conformation which accounts for all experimental data on EAAT anion currents reported so far We here review recent findings on how EAATs accommodate a transporter and a channel in one single protein
Keywords: