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| Hauptseite > Publikationsdatenbank > Allosteric modulation of proton binding confers Cl- activation and glutamate selectivity to vesicular glutamate transporters > print |
| Hauptseite > Publikationsdatenbank > Allosteric modulation of proton binding confers Cl- activation and glutamate selectivity to vesicular glutamate transporters > print |
| 001 | 1044114 | ||
| 005 | 20260123203311.0 | ||
| 024 | 7 | _ | |a 10.1371/journal.pcbi.1013214 |2 doi |
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| 100 | 1 | _ | |a Borghans, Bart |0 P:(DE-Juel1)176659 |b 0 |u fzj |
| 245 | _ | _ | |a Allosteric modulation of proton binding confers Cl- activation and glutamate selectivity to vesicular glutamate transporters |
| 260 | _ | _ | |a San Francisco, Calif. |c 2025 |b Public Library of Science |
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| 520 | _ | _ | |a Vesicular glutamate transporters (VGLUTs) fill synaptic vesicles with glutamate andremove luminal Cl- via an additional anion channel mode. Both of these transportfunctions are stimulated by luminal acidification, luminal-positive membrane potential,and luminal Cl-. We studied VGLUT1 transporter/channel activation using acombination of heterologous expression, cellular electrophysiology, fast solutionexchange, and mathematical modeling. Cl- channel gating can be described with akinetic scheme that includes two protonation sites and distinct opening, closing, andCl--binding rates for each protonation state. Cl- binding promotes channel openingby modifying the pKa values of the protonation sites and rates of pore opening andclosure. VGLUT1 transports glutamate and aspartate at distinct stoichiometries:H+-glutamate exchange at 1:1 stoichiometry and aspartate uniport. Neurotransmittertransport with variable stoichiometry can be described with an alternating accessmodel that assumes that transporters without substrate translocate in the doubly protonatedstate to the inward-facing conformation and return with the bound amino acidsubstrate as either singly or doubly protonated. Glutamate, but not aspartate, promotesthe release of one proton from inward-facing VGLUT1, resulting in preferentialH+-coupled glutamate exchange. Cl- stimulates glutamate transport by making theglutamate-binding site accessible to cytoplasmic glutamate and by facilitating transitionsto the inward-facing conformation after outward substrate release. We concludethat allosteric modification of transporter protonation by Cl- is crucial for both VGLUT1transport functions. |
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| 700 | 1 | _ | |a Kortzak, Daniel |0 P:(DE-Juel1)157846 |b 1 |
| 700 | 1 | _ | |a Longo, Piersilvio |0 P:(DE-Juel1)174421 |b 2 |u fzj |
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| 700 | 1 | _ | |a Fahlke, Christoph |0 P:(DE-Juel1)136837 |b 5 |e Corresponding author |
| 773 | _ | _ | |a 10.1371/journal.pcbi.1013214 |g Vol. 21, no. 6, p. e1013214 - |0 PERI:(DE-600)2193340-6 |n 6 |p e1013214 - |t PLoS Computational Biology |v 21 |y 2025 |x 1553-734X |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/1044114/files/PLOS_Borghans_Kortzak_Longo_Machtens_Fahlke_06_2025.pdf |y OpenAccess |
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