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@ARTICLE{Kortzak:865082,
      author       = {Kortzak, Daniel and Alleva, Claudia and Weyand, Ingo and
                      Ewers, David and Zimmermann, Meike I and Franzen, Arne and
                      Machtens, Jan‐Philipp and Fahlke, Christoph},
      title        = {{A}llosteric gate modulation confers {K} + coupling in
                      glutamate transporters},
      journal      = {The EMBO journal},
      volume       = {38},
      number       = {19},
      issn         = {1460-2075},
      address      = {Hoboken, NJ [u.a.]},
      publisher    = {Wiley},
      reportid     = {FZJ-2019-04644},
      pages        = {e101468},
      year         = {2019},
      abstract     = {Excitatory amino acid transporters (EAAT s) mediate glial
                      and neuronal glutamate uptake to terminate synaptic
                      transmission and to ensure low resting glutamate
                      concentrations. Effective glutamate uptake is achieved by
                      cotransport with 3 Na+ and 1 H+, in exchange with 1 K+. The
                      underlying principles of this complex transport
                      stoichiometry remain poorly understood. We use molecular
                      dynamics simulations and electrophysiological experiments to
                      elucidate how mammalian EAAT s harness K+ gradients, unlike
                      their K+‐independent prokaryotic homologues. Glutamate
                      transport is achieved via elevator‐like translocation of
                      the transport domain. In EAAT s, glutamate‐free
                      re‐translocation is prevented by an external gate
                      remaining open until K+ binding closes and locks the gate.
                      Prokaryotic GltPh contains the same K+‐binding site, but
                      the gate can close without K+. Our study provides a
                      comprehensive description of K+‐dependent glutamate
                      transport and reveals a hitherto unknown allosteric coupling
                      mechanism that permits adaptions of the transport
                      stoichiometry without affecting ion or substrate binding.},
      cin          = {ICS-4 / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-4-20110106 / $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      Mechanisms of Ca2+-activated Cl- channels and lipid
                      scramblases of the TMEM16 family $(jics41_20161101)$ /
                      Molecular dynamics of the SLC26 family of ion channels and
                      transporters $(jara0177_20171101)$ / Multiscale simulations
                      of voltage-gated sodium channel complexes and clusters
                      $(jics42_20181101)$ / MOLECULAR MODELLING OF BIFUNCTIONAL
                      MEMBRANE TRANSPORT PROTEINS $(jics40_20190501)$ / Molecular
                      dynamics simulations of P2X receptors $(jara0180_20200501)$},
      pid          = {G:(DE-HGF)POF3-551 / $G:(DE-Juel1)jics41_20161101$ /
                      $G:(DE-Juel1)jara0177_20171101$ /
                      $G:(DE-Juel1)jics42_20181101$ /
                      $G:(DE-Juel1)jics40_20190501$ /
                      $G:(DE-Juel1)jara0180_20200501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31506973},
      UT           = {WOS:000486931900001},
      doi          = {10.15252/embj.2019101468},
      url          = {https://juser.fz-juelich.de/record/865082},
}