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@ARTICLE{Kolen:1009116,
      author       = {Kolen, Bettina and Borghans, Bart and Kortzak, Daniel and
                      Lugo, Victor and Hannack, Cora and Guzman, Raul and Ullah,
                      Ghanim and Fahlke, Christoph},
      title        = {{V}esicular glutamate transporters are {H}+-anion
                      exchangers that operate at variable stoichiometry},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2023-02646},
      pages        = {2723},
      year         = {2023},
      note         = {This workwas supported by the Deutsche
                      Forschungsgemeinschaft (GermanResearch Foundation) to Ch.F.
                      (FA 301/15–2) as part of Research UnitFOR 2518, DynIon; to
                      Ch.F. and G.U. as part of the Research Unit FOR2795, to REG
                      (GU 2042/2-1), and by the NIH to G.U. (R01 AG053988).},
      abstract     = {Vesicular glutamate transporters accumulate glutamate in
                      synaptic vesicles, where they also function as a major Cl-
                      efflux pathway. Here we combine heterologous expression and
                      cellular electrophysiology with mathematical modeling to
                      understand the mechanisms underlying this dual function of
                      rat VGLUT1. When glutamate is the main cytoplasmic anion,
                      VGLUT1 functions as H+-glutamate exchanger, with a transport
                      rate of around 600 s−1 at −160 mV. Transport of other
                      large anions, including aspartate, is not stoichiometrically
                      coupled to H+ transport, and Cl- permeates VGLUT1 through an
                      aqueous anion channel with unitary transport rates of 1.5 ×
                      105 s−1 at −160 mV. Mathematical modeling reveals that
                      H+ coupling is sufficient for selective glutamate
                      accumulation in model vesicles and that VGLUT Cl- channel
                      function increases the transport efficiency by accelerating
                      glutamate accumulation and reducing ATP-driven H+ transport.
                      In summary, we provide evidence that VGLUT1 functions as
                      H+-glutamate exchanger that is partially or fully uncoupled
                      by other anions.},
      cin          = {IBI-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-1-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37169755},
      UT           = {WOS:000992465700006},
      doi          = {10.1038/s41467-023-38340-9},
      url          = {https://juser.fz-juelich.de/record/1009116},
}