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@ARTICLE{Fahlke:808781,
author = {Fahlke, Christoph and Kortzak, Daniel and Machtens,
Jan-Philipp},
title = {{M}olecular physiology of {EAAT} anion channels},
journal = {Pflügers Archiv},
volume = {468},
number = {3},
issn = {1432-2013},
address = {Berlin},
publisher = {Springer},
reportid = {FZJ-2016-02397},
pages = {491 - 502},
year = {2016},
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 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.},
cin = {ICS-4},
ddc = {610},
cid = {I:(DE-Juel1)ICS-4-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000370177200010},
pubmed = {pmid:26687113},
doi = {10.1007/s00424-015-1768-3},
url = {https://juser.fz-juelich.de/record/808781},
}