TY  - JOUR
AU  - Fahlke, Christoph
AU  - Kortzak, Daniel
AU  - Machtens, Jan-Philipp
TI  - Molecular physiology of EAAT anion channels
JO  - Pflügers Archiv
VL  - 468
IS  - 3
SN  - 1432-2013
CY  - Berlin
PB  - Springer
M1  - FZJ-2016-02397
SP  - 491 - 502
PY  - 2016
AB  - 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 so-called excitatory amino acid transporters (EAAT1–5). EAATs are prototypic members of the growing number of dual-function 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 simulation-guided mutagenesis and experimental analysis identified a novel anion-conducting 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000370177200010
C6  - pmid:26687113
DO  - DOI:10.1007/s00424-015-1768-3
UR  - https://juser.fz-juelich.de/record/808781
ER  -