메뉴 건너뛰기




Volumn 468, Issue 3, 2016, Pages 491-502

Molecular physiology of EAAT anion channels

Author keywords

Anion channel; Computational electrophysiology; Glutamate transport; Molecular dynamics simulation

Indexed keywords

ANION CHANNEL; EXCITATORY AMINO ACID TRANSPORTER; GLUTAMATE TRANSPORTER; GLUTAMIC ACID;

EID: 84957954771     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-015-1768-3     Document Type: Review
Times cited : (41)

References (80)
  • 1
    • 84872333816 scopus 로고    scopus 로고
    • Allosteric modulation of an excitatory amino acid transporter: the subtype-selective inhibitor UCPH-101 exerts sustained inhibition of EAAT1 through an intramonomeric site in the trimerization domain
    • PID: 23325245
    • Abrahamsen B, Schneider N, Erichsen MN, Huynh TH, Fahlke C, Bunch L, Jensen AA (2013) Allosteric modulation of an excitatory amino acid transporter: the subtype-selective inhibitor UCPH-101 exerts sustained inhibition of EAAT1 through an intramonomeric site in the trimerization domain. J Neurosci 33:1068–1087. doi:10.1523/jneurosci.3396-12.2013
    • (2013) J Neurosci , vol.33 , pp. 1068-1087
    • Abrahamsen, B.1    Schneider, N.2    Erichsen, M.N.3    Huynh, T.H.4    Fahlke, C.5    Bunch, L.6    Jensen, A.A.7
  • 2
    • 66049097472 scopus 로고    scopus 로고
    • Channel-like slippage modes in the human anion/proton exchanger ClC-4
    • PID: 19364886
    • Alekov A, Fahlke C (2009) Channel-like slippage modes in the human anion/proton exchanger ClC-4. J Gen Physiol 133:485–496
    • (2009) J Gen Physiol , vol.133 , pp. 485-496
    • Alekov, A.1    Fahlke, C.2
  • 3
    • 0030932152 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance
    • PID: 9108121
    • Arriza JL, Eliasof S, Kavanaugh MP, Amara SG (1997) Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance. Proc Natl Acad Sci USA 94:4155–4160
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4155-4160
    • Arriza, J.L.1    Eliasof, S.2    Kavanaugh, M.P.3    Amara, S.G.4
  • 5
    • 0036896927 scopus 로고    scopus 로고
    • Comparison of coupled and uncoupled currents during glutamate uptake by GLT-1 transporters
    • PID: 12451116
    • Bergles DE, Tzingounis AV, Jahr CE (2002) Comparison of coupled and uncoupled currents during glutamate uptake by GLT-1 transporters. J Neurosci 22:10153–10162
    • (2002) J Neurosci , vol.22 , pp. 10153-10162
    • Bergles, D.E.1    Tzingounis, A.V.2    Jahr, C.E.3
  • 6
    • 1642494714 scopus 로고    scopus 로고
    • Arginine-445 controls the coupling between glutamate and cations in the neuronal glutamate transporter EAAC-1
    • PID: 14594797
    • Borre L, Kanner BI (2004) Arginine-445 controls the coupling between glutamate and cations in the neuronal glutamate transporter EAAC-1. J Biol Chem 279:2513–2519
    • (2004) J Biol Chem , vol.279 , pp. 2513-2519
    • Borre, L.1    Kanner, B.I.2
  • 7
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • PID: 17230192
    • Boudker O, Ryan RM, Yernool D, Shimamoto K, Gouaux E (2007) Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445:387–393
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 8
    • 84905658050 scopus 로고    scopus 로고
    • The domain interface of the human glutamate transporter EAAT1 mediates chloride permeation
    • PID: 25099801
    • Cater RJ, Vandenberg RJ, Ryan RM (2014) The domain interface of the human glutamate transporter EAAT1 mediates chloride permeation. Biophys J 107:621–629. doi:10.1016/j.bpj.2014.05.046
    • (2014) Biophys J , vol.107 , pp. 621-629
    • Cater, R.J.1    Vandenberg, R.J.2    Ryan, R.M.3
  • 9
    • 0344999542 scopus 로고
    • Concentrative uptake of amino acids by the Ehrlich mouse ascites carcinoma cell
    • PID: 14927593
    • Christensen HN, Riggs TR (1952) Concentrative uptake of amino acids by the Ehrlich mouse ascites carcinoma cell. J Biol Chem 194:57–68
    • (1952) J Biol Chem , vol.194 , pp. 57-68
    • Christensen, H.N.1    Riggs, T.R.2
  • 10
    • 0017439356 scopus 로고
    • The gradient hypothesis and other models of carrier-mediated active transport
    • PID: 322241
    • Crane RK (1977) The gradient hypothesis and other models of carrier-mediated active transport. Rev Physiol Biochem Pharmacol 78:99–159
    • (1977) Rev Physiol Biochem Pharmacol , vol.78 , pp. 99-159
    • Crane, R.K.1
  • 11
    • 73949133608 scopus 로고    scopus 로고
    • Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats
    • PID: 19926849
    • Crisman TJ, Qu S, Kanner BI, Forrest LR (2009) Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats. Proc Natl Acad Sci USA 106:20752–20757
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20752-20757
    • Crisman, T.J.1    Qu, S.2    Kanner, B.I.3    Forrest, L.R.4
  • 12
    • 0035001341 scopus 로고    scopus 로고
    • Glutamate uptake
    • Danbolt NC (2001) Glutamate uptake. Progr Neurobiol 65:1–105
    • (2001) Progr Neurobiol , vol.65 , pp. 1-105
    • Danbolt, N.C.1
  • 13
  • 14
    • 84885606528 scopus 로고    scopus 로고
    • Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters
    • PID: 24091978
    • Erkens GB, Hanelt I, Goudsmits JM, Slotboom DJ, van Oijen AM (2013) Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters. Nature 502:119–123. doi:10.1038/nature12538
    • (2013) Nature , vol.502 , pp. 119-123
    • Erkens, G.B.1    Hanelt, I.2    Goudsmits, J.M.3    Slotboom, D.J.4    van Oijen, A.M.5
  • 15
    • 84880653278 scopus 로고    scopus 로고
    • Induced fit substrate binding to an archeal glutamate transporter homologue
    • PID: 23840066
    • Ewers D, Becher T, Machtens JP, Weyand I, Fahlke C (2013) Induced fit substrate binding to an archeal glutamate transporter homologue. Proc Natl Acad Sci USA 110:12486–12491. doi:10.1073/pnas.1300772110
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 12486-12491
    • Ewers, D.1    Becher, T.2    Machtens, J.P.3    Weyand, I.4    Fahlke, C.5
  • 16
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • PID: 7791878
    • Fairman WA, Vandenberg RJ, Arriza JL, Kavanaugh MP, Amara SG (1995) An excitatory amino-acid transporter with properties of a ligand-gated chloride channel. Nature 375:599–603
    • (1995) Nature , vol.375 , pp. 599-603
    • Fairman, W.A.1    Vandenberg, R.J.2    Arriza, J.L.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 17
    • 79960311633 scopus 로고    scopus 로고
    • The discovery of slowness: low-capacity transport and slow anion channel gating by the glutamate transporter EAAT5
    • PID: 21641307
    • Gameiro A, Braams S, Rauen T, Grewer C (2011) The discovery of slowness: low-capacity transport and slow anion channel gating by the glutamate transporter EAAT5. Biophys J 100:2623–2632
    • (2011) Biophys J , vol.100 , pp. 2623-2632
    • Gameiro, A.1    Braams, S.2    Rauen, T.3    Grewer, C.4
  • 19
    • 24344507684 scopus 로고    scopus 로고
    • Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other
    • PID: 16128593
    • Grewer C, Balani P, Weidenfeller C, Bartusel T, Tao Z, Rauen T (2005) Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other. Biochemistry 44:11913–11923
    • (2005) Biochemistry , vol.44 , pp. 11913-11923
    • Grewer, C.1    Balani, P.2    Weidenfeller, C.3    Bartusel, T.4    Tao, Z.5    Rauen, T.6
  • 20
    • 0034662861 scopus 로고    scopus 로고
    • Glutamate translocation of the neuronal glutamate transporter EAAC1 occurs within milliseconds
    • PID: 10931942
    • Grewer C, Watzke N, Wiessner M, Rauen T (2000) Glutamate translocation of the neuronal glutamate transporter EAAC1 occurs within milliseconds. Proc Natl Acad Sci USA 97:9706–9711
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9706-9711
    • Grewer, C.1    Watzke, N.2    Wiessner, M.3    Rauen, T.4
  • 25
    • 84862025150 scopus 로고    scopus 로고
    • Neutralizing aspartate 83 modifies substrate translocation of excitatory amino acid transporter 3 (EAAT3) glutamate transporters
    • PID: 22532568
    • Hotzy J, Machtens JP, Fahlke C (2012) Neutralizing aspartate 83 modifies substrate translocation of excitatory amino acid transporter 3 (EAAT3) glutamate transporters. J Biol Chem 287:20016–20026
    • (2012) J Biol Chem , vol.287 , pp. 20016-20026
    • Hotzy, J.1    Machtens, J.P.2    Fahlke, C.3
  • 26
    • 34548286807 scopus 로고    scopus 로고
    • Mutations in transmembrane domains 5 and 7 of the human excitatory amino acid transporter 1 affect the substrate-activated anion channel
    • PID: 17676873
    • Huang S, Vandenberg RJ (2007) Mutations in transmembrane domains 5 and 7 of the human excitatory amino acid transporter 1 affect the substrate-activated anion channel. Biochemistry 46:9685–9692
    • (2007) Biochemistry , vol.46 , pp. 9685-9692
    • Huang, S.1    Vandenberg, R.J.2
  • 27
    • 51649088013 scopus 로고    scopus 로고
    • Dynamics of the extracellular gate and ion-substrate coupling in the glutamate transporter
    • PID: 18515371
    • Huang Z, Tajkhorshid E (2008) Dynamics of the extracellular gate and ion-substrate coupling in the glutamate transporter. Biophys J 95:2292–2300
    • (2008) Biophys J , vol.95 , pp. 2292-2300
    • Huang, Z.1    Tajkhorshid, E.2
  • 28
    • 84922522810 scopus 로고    scopus 로고
    • Excitatory amino acid transporters: recent insights into molecular mechanisms, novel modes of modulation and new therapeutic possibilities
    • PID: 25466154
    • Jensen AA, Fahlke C, Bjorn-Yoshimoto WE, Bunch L (2015) Excitatory amino acid transporters: recent insights into molecular mechanisms, novel modes of modulation and new therapeutic possibilities. Curr Opin Pharmacol 20:116–123. doi:10.1016/j.coph.2014.10.008
    • (2015) Curr Opin Pharmacol , vol.20 , pp. 116-123
    • Jensen, A.A.1    Fahlke, C.2    Bjorn-Yoshimoto, W.E.3    Bunch, L.4
  • 29
    • 84885401279 scopus 로고    scopus 로고
    • Crystal structure of a substrate-free aspartate transporter
    • PID: 24013209
    • Jensen S, Guskov A, Rempel S, Hanelt I, Slotboom DJ (2013) Crystal structure of a substrate-free aspartate transporter. Nat Struct Mol Biol 20(10):1224–1226. doi:10.1038/nsmb.2663
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.10 , pp. 1224-1226
    • Jensen, S.1    Guskov, A.2    Rempel, S.3    Hanelt, I.4    Slotboom, D.J.5
  • 31
    • 33947318986 scopus 로고    scopus 로고
    • The glutamate-activated anion conductance in excitatory amino acid transporters is gated independently by the individual subunits
    • PID: 17360917
    • Koch HP, Brown RL, Larsson HP (2007) The glutamate-activated anion conductance in excitatory amino acid transporters is gated independently by the individual subunits. J Neurosci 27:2943–2947
    • (2007) J Neurosci , vol.27 , pp. 2943-2947
    • Koch, H.P.1    Brown, R.L.2    Larsson, H.P.3
  • 32
    • 77954929051 scopus 로고    scopus 로고
    • A conserved aspartate determines pore properties of anion channels associated with excitatory amino acid transporter 4 (EAAT4)
    • PID: 20519505
    • Kovermann P, Machtens JP, Ewers D, Fahlke C (2010) A conserved aspartate determines pore properties of anion channels associated with excitatory amino acid transporter 4 (EAAT4). J Biol Chem 285:23676–23686
    • (2010) J Biol Chem , vol.285 , pp. 23676-23686
    • Kovermann, P.1    Machtens, J.P.2    Ewers, D.3    Fahlke, C.4
  • 33
    • 0030030516 scopus 로고    scopus 로고
    • Noise analysis of the glutamate-activated current in photoreceptors
    • PID: 8789090
    • Larsson HP, Picaud SA, Werblin FS, Lecar H (1996) Noise analysis of the glutamate-activated current in photoreceptors. Biophys J 70:733–742
    • (1996) Biophys J , vol.70 , pp. 733-742
    • Larsson, H.P.1    Picaud, S.A.2    Werblin, F.S.3    Lecar, H.4
  • 34
    • 33947308773 scopus 로고    scopus 로고
    • The glutamate and chloride permeation pathways are colocalized in individual neuronal glutamate transporter subunits
    • PID: 17360916
    • Leary GP, Stone EF, Holley DC, Kavanaugh MP (2007) The glutamate and chloride permeation pathways are colocalized in individual neuronal glutamate transporter subunits. J Neurosci 27:2938–2942
    • (2007) J Neurosci , vol.27 , pp. 2938-2942
    • Leary, G.P.1    Stone, E.F.2    Holley, D.C.3    Kavanaugh, M.P.4
  • 35
    • 78751506350 scopus 로고    scopus 로고
    • Regulation of glial glutamate transporters by C-terminal domains
    • PID: 21097502
    • Leinenweber A, Machtens JP, Begemann B, Fahlke C (2011) Regulation of glial glutamate transporters by C-terminal domains. J Biol Chem 286:1927–1937
    • (2011) J Biol Chem , vol.286 , pp. 1927-1937
    • Leinenweber, A.1    Machtens, J.P.2    Begemann, B.3    Fahlke, C.4
  • 36
    • 0030292906 scopus 로고    scopus 로고
    • Listening to neurotransmitter transporters
    • PID: 8938113
    • Lester HA, Cao Y, Mager S (1996) Listening to neurotransmitter transporters. Neuron 17:807–810
    • (1996) Neuron , vol.17 , pp. 807-810
    • Lester, H.A.1    Cao, Y.2    Mager, S.3
  • 37
    • 84877317987 scopus 로고    scopus 로고
    • Transient formation of water-conducting states in membrane transporters
    • PID: 23610412
    • Li J, Shaikh SA, Enkavi G, Wen PC, Huang Z, Tajkhorshid E (2013) Transient formation of water-conducting states in membrane transporters. Proc Natl Acad Sci USA 110:7696–7701. doi:10.1073/pnas.1218986110
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 7696-7701
    • Li, J.1    Shaikh, S.A.2    Enkavi, G.3    Wen, P.C.4    Huang, Z.5    Tajkhorshid, E.6
  • 39
    • 84455210220 scopus 로고    scopus 로고
    • Noise analysis to study unitary properties of transporter-associated ion channels
    • PID: 21849820
    • Machtens JP, Fahlke C, Kovermann P (2011) Noise analysis to study unitary properties of transporter-associated ion channels. Channels 5:468–472
    • (2011) Channels , vol.5 , pp. 468-472
    • Machtens, J.P.1    Fahlke, C.2    Kovermann, P.3
  • 41
    • 79959887884 scopus 로고    scopus 로고
    • Substrate-dependent gating of anion channels associated with excitatory amino acid transporter 4
    • PID: 21572047
    • Machtens JP, Kovermann P, Fahlke C (2011) Substrate-dependent gating of anion channels associated with excitatory amino acid transporter 4. J Biol Chem 286:23780–23788. doi:10.1074/jbc.M110.207514
    • (2011) J Biol Chem , vol.286 , pp. 23780-23788
    • Machtens, J.P.1    Kovermann, P.2    Fahlke, C.3
  • 42
    • 4544342928 scopus 로고    scopus 로고
    • Potassium channels and the atomic basis of selective ion conduction (Nobel Lecture)
    • MacKinnon R (2004) Potassium channels and the atomic basis of selective ion conduction (Nobel Lecture). Angew Chem (Intern ed in English) 43:4265–4277. doi:10.1002/anie.200400662
    • (2004) Angew Chem (Intern ed in English) , vol.43 , pp. 4265-4277
    • MacKinnon, R.1
  • 44
    • 0027537292 scopus 로고
    • Steady states, charge movements, and rates for a cloned GABA transporter expressed in Xenopus oocytes
    • PID: 7679914
    • Mager S, Naeve J, Quick M, Labarca C, Davidson N, Lester HA (1993) Steady states, charge movements, and rates for a cloned GABA transporter expressed in Xenopus oocytes. Neuron 10:177–188
    • (1993) Neuron , vol.10 , pp. 177-188
    • Mager, S.1    Naeve, J.2    Quick, M.3    Labarca, C.4    Davidson, N.5    Lester, H.A.6
  • 45
    • 0346118920 scopus 로고    scopus 로고
    • Glutamate modifies ion conduction and voltage-dependent gating of excitatory amino acid transporter-associated anion channels
    • PID: 14506254
    • Melzer N, Biela A, Fahlke C (2003) Glutamate modifies ion conduction and voltage-dependent gating of excitatory amino acid transporter-associated anion channels. J Biol Chem 278:50112–50119
    • (2003) J Biol Chem , vol.278 , pp. 50112-50119
    • Melzer, N.1    Biela, A.2    Fahlke, C.3
  • 46
    • 30044432200 scopus 로고    scopus 로고
    • A dynamic switch between inhibitory and excitatory currents in a neuronal glutamate transporter
    • PID: 16365297
    • Melzer N, Torres-Salazar D, Fahlke C (2005) A dynamic switch between inhibitory and excitatory currents in a neuronal glutamate transporter. Proc Natl Acad Sci USA 102:19214–19218
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 19214-19218
    • Melzer, N.1    Torres-Salazar, D.2    Fahlke, C.3
  • 47
    • 28244490270 scopus 로고    scopus 로고
    • The glutamate transporter subtypes EAAT4 and EAATs 1-3 transport glutamate with dramatically different kinetics and voltage dependence but share a common uptake mechanism
    • PID: 16316976
    • Mim C, Balani P, Rauen T, Grewer C (2005) The glutamate transporter subtypes EAAT4 and EAATs 1-3 transport glutamate with dramatically different kinetics and voltage dependence but share a common uptake mechanism. J Gen Physiol 126:571–589
    • (2005) J Gen Physiol , vol.126 , pp. 571-589
    • Mim, C.1    Balani, P.2    Rauen, T.3    Grewer, C.4
  • 48
    • 0036843663 scopus 로고    scopus 로고
    • The significance of molecular slips in transport systems
    • PID: 12415305
    • Nelson N, Sacher A, Nelson H (2002) The significance of molecular slips in transport systems. Nat Rev Mol Cell Biol 3:876–881
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 876-881
    • Nelson, N.1    Sacher, A.2    Nelson, H.3
  • 49
    • 0037318653 scopus 로고    scopus 로고
    • Amazing chloride channels: an overview
    • PID: 12558550
    • Nilius B, Droogmans G (2003) Amazing chloride channels: an overview. Acta Physiol Scand 177:119–147
    • (2003) Acta Physiol Scand , vol.177 , pp. 119-147
    • Nilius, B.1    Droogmans, G.2
  • 50
    • 0032531028 scopus 로고    scopus 로고
    • Anion currents and predicted glutamate flux through a neuronal glutamate transporter
    • Otis TS, Jahr CE (1998) Anion currents and predicted glutamate flux through a neuronal glutamate transporter. J Neurosc 18:7099–7110
    • (1998) J Neurosc , vol.18 , pp. 7099-7110
    • Otis, T.S.1    Jahr, C.E.2
  • 51
    • 0034655871 scopus 로고    scopus 로고
    • Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2
    • PID: 10751425
    • Otis TS, Kavanaugh MP (2000) Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2. J Neurosci 20:2749–2757
    • (2000) J Neurosci , vol.20 , pp. 2749-2757
    • Otis, T.S.1    Kavanaugh, M.P.2
  • 52
    • 0037741030 scopus 로고    scopus 로고
    • Synaptic activation of presynaptic glutamate transporter currents in nerve terminals
    • PID: 12832505
    • Palmer MJ, Taschenberger H, Hull C, Tremere L, von Gersdorff H (2003) Synaptic activation of presynaptic glutamate transporter currents in nerve terminals. J Neurosci 23:4831–4841
    • (2003) J Neurosci , vol.23 , pp. 4831-4841
    • Palmer, M.J.1    Taschenberger, H.2    Hull, C.3    Tremere, L.4    von Gersdorff, H.5
  • 53
    • 0028786382 scopus 로고
    • Glutamate-gated chloride channel with glutamate-transporter-like properties in cone photoreceptors of the tiger salamander
    • PID: 8989410
    • Picaud SA, Larsson HP, Grant GB, Lecar H, Werblin FS (1995) Glutamate-gated chloride channel with glutamate-transporter-like properties in cone photoreceptors of the tiger salamander. J Neurophysiol 74:1760–1771
    • (1995) J Neurophysiol , vol.74 , pp. 1760-1771
    • Picaud, S.A.1    Larsson, H.P.2    Grant, G.B.3    Lecar, H.4    Werblin, F.S.5
  • 54
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • PID: 19924125
    • Reyes N, Ginter C, Boudker O (2009) Transport mechanism of a bacterial homologue of glutamate transporters. Nature 462:880–885
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 56
    • 34247648737 scopus 로고    scopus 로고
    • The uncoupled chloride conductance of a bacterial glutamate transporter homolog
    • PID: 17435767
    • Ryan RM, Mindell JA (2007) The uncoupled chloride conductance of a bacterial glutamate transporter homolog. Nat Struct Mol Biol 14:365–371
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 365-371
    • Ryan, R.M.1    Mindell, J.A.2
  • 57
    • 2442693929 scopus 로고    scopus 로고
    • The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway
    • PID: 14982939
    • Ryan RM, Mitrovic AD, Vandenberg RJ (2004) The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway. J Biol Chem 279:20742–20751
    • (2004) J Biol Chem , vol.279 , pp. 20742-20751
    • Ryan, R.M.1    Mitrovic, A.D.2    Vandenberg, R.J.3
  • 58
    • 0037134466 scopus 로고    scopus 로고
    • Distinct conformational states mediate the transport and anion channel properties of the glutamate transporter EAAT-1
    • PID: 11815608
    • Ryan RM, Vandenberg RJ (2002) Distinct conformational states mediate the transport and anion channel properties of the glutamate transporter EAAT-1. J Biol Chem 277:13494–13500
    • (2002) J Biol Chem , vol.277 , pp. 13494-13500
    • Ryan, R.M.1    Vandenberg, R.J.2
  • 59
    • 58849125253 scopus 로고    scopus 로고
    • A chloride conductance in VGLUT1 underlies maximal glutamate loading into synaptic vesicles
    • PID: 19169251
    • Schenck S, Wojcik SM, Brose N, Takamori S (2009) A chloride conductance in VGLUT1 underlies maximal glutamate loading into synaptic vesicles. Nat Neurosci 12:156–162. doi:10.1038/nn.2248
    • (2009) Nat Neurosci , vol.12 , pp. 156-162
    • Schenck, S.1    Wojcik, S.M.2    Brose, N.3    Takamori, S.4
  • 60
    • 84892667473 scopus 로고    scopus 로고
    • Functional properties of the retinal glutamate transporters GLT-1c and EAAT5
    • PID: 24307171
    • Schneider N, Cordeiro S, Machtens JP, Braams S, Rauen T, Fahlke C (2014) Functional properties of the retinal glutamate transporters GLT-1c and EAAT5. J Biol Chem 289:1815. doi:10.1074/jbc.M113.517177
    • (2014) J Biol Chem , vol.289 , pp. 1815
    • Schneider, N.1    Cordeiro, S.2    Machtens, J.P.3    Braams, S.4    Rauen, T.5    Fahlke, C.6
  • 61
    • 0035909950 scopus 로고    scopus 로고
    • Sulfhydryl modification of V449C in the glutamate transporter EAAT1 abolishes substrate transport but not the substrate-gated anion conductance
    • PID: 11752470
    • Seal RP, Shigeri Y, Eliasof S, Leighton BH, Amara SG (2001) Sulfhydryl modification of V449C in the glutamate transporter EAAT1 abolishes substrate transport but not the substrate-gated anion conductance. Proc Natl Acad Sci USA 98:15324–15329
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15324-15329
    • Seal, R.P.1    Shigeri, Y.2    Eliasof, S.3    Leighton, B.H.4    Amara, S.G.5
  • 62
    • 84899011312 scopus 로고    scopus 로고
    • Disulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductance
    • PID: 24584931
    • Shabaneh M, Rosental N, Kanner BI (2014) Disulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductance. J Biol Chem 289:11175–11182. doi:10.1074/jbc.M114.550277
    • (2014) J Biol Chem , vol.289 , pp. 11175-11182
    • Shabaneh, M.1    Rosental, N.2    Kanner, B.I.3
  • 63
    • 57649119782 scopus 로고    scopus 로고
    • Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter
    • PID: 18678877
    • Shrivastava IH, Jiang J, Amara SG, Bahar I (2008) Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter. J Biol Chem 283:28680–28690. doi:10.1074/jbc.M800889200
    • (2008) J Biol Chem , vol.283 , pp. 28680-28690
    • Shrivastava, I.H.1    Jiang, J.2    Amara, S.G.3    Bahar, I.4
  • 64
    • 84861090698 scopus 로고    scopus 로고
    • Structural intermediates in a model of the substrate translocation path of the bacterial glutamate transporter homologue GltPh
    • PID: 22494242
    • Stolzenberg S, Khelashvili G, Weinstein H (2012) Structural intermediates in a model of the substrate translocation path of the bacterial glutamate transporter homologue GltPh. J Phys Chem B 116:5372–5383
    • (2012) J Phys Chem B , vol.116 , pp. 5372-5383
    • Stolzenberg, S.1    Khelashvili, G.2    Weinstein, H.3
  • 65
    • 33947726549 scopus 로고    scopus 로고
    • + binding to the glutamate transporter EAAC1
    • PID: 17389249
    • + binding to the glutamate transporter EAAC1. J Gen Physiol 129:331–344
    • (2007) J Gen Physiol , vol.129 , pp. 331-344
    • Tao, Z.1    Grewer, C.2
  • 66
    • 77952907248 scopus 로고    scopus 로고
    • Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101
    • PID: 20378543
    • Tao Z, Rosental N, Kanner BI, Gameiro A, Mwaura J, Grewer C (2010) Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101. J Biol Chem 285:17725–17733
    • (2010) J Biol Chem , vol.285 , pp. 17725-17733
    • Tao, Z.1    Rosental, N.2    Kanner, B.I.3    Gameiro, A.4    Mwaura, J.5    Grewer, C.6
  • 67
    • 33744518437 scopus 로고    scopus 로고
    • + to the glutamate-free form and cycling of the glutamate transporter EAAC1
    • PID: 16478724
    • + to the glutamate-free form and cycling of the glutamate transporter EAAC1. J Biol Chem 281:10263–10272
    • (2006) J Biol Chem , vol.281 , pp. 10263-10272
    • Tao, Z.1    Zhang, Z.2    Grewer, C.3
  • 68
    • 36849045104 scopus 로고    scopus 로고
    • Neuronal glutamate transporters vary in substrate transport rate but not in unitary anion channel conductance
    • PID: 17908688
    • Torres-Salazar D, Fahlke C (2007) Neuronal glutamate transporters vary in substrate transport rate but not in unitary anion channel conductance. J Biol Chem 282:34719–34726
    • (2007) J Biol Chem , vol.282 , pp. 34719-34726
    • Torres-Salazar, D.1    Fahlke, C.2
  • 69
    • 84942860897 scopus 로고    scopus 로고
    • A mutation in transmembrane domain 7 (TM7) of excitatory amino acid transporters disrupts the substrate-dependent gating of the intrinsic anion conductance and drives the channel into a constitutively open state
    • PID: 26203187
    • Torres-Salazar D, Jiang J, Divito CB, Garcia-Olivares J, Amara SG (2015) A mutation in transmembrane domain 7 (TM7) of excitatory amino acid transporters disrupts the substrate-dependent gating of the intrinsic anion conductance and drives the channel into a constitutively open state. J Biol Chem 290:22977–22990. doi:10.1074/jbc.M115.660860
    • (2015) J Biol Chem , vol.290 , pp. 22977-22990
    • Torres-Salazar, D.1    Jiang, J.2    Divito, C.B.3    Garcia-Olivares, J.4    Amara, S.G.5
  • 70
    • 80053280649 scopus 로고    scopus 로고
    • Water and urea permeation pathways of the human excitatory amino acid transporter EAAT1
    • PID: 21732909
    • Vandenberg RJ, Handford CA, Campbell EM, Ryan RM, Yool AJ (2011) Water and urea permeation pathways of the human excitatory amino acid transporter EAAT1. Biochem J 439:333–340. doi:10.1042/bj20110905
    • (2011) Biochem J , vol.439 , pp. 333-340
    • Vandenberg, R.J.1    Handford, C.A.2    Campbell, E.M.3    Ryan, R.M.4    Yool, A.J.5
  • 71
    • 84857992685 scopus 로고    scopus 로고
    • Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog
    • PID: 22343718
    • Verdon G, Boudker O (2012) Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog. Nat Struct Mol Biol 19:355–357
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 355-357
    • Verdon, G.1    Boudker, O.2
  • 72
    • 84901049540 scopus 로고    scopus 로고
    • Coupled ion binding and structural transitions along the transport cycle of glutamate transporters
    • PID: 24842876
    • Verdon G, Oh S, Serio RN, Boudker O (2014) Coupled ion binding and structural transitions along the transport cycle of glutamate transporters. eLife 3:e02283. doi:10.7554/eLife.02283
    • (2014) ELife , vol.3 , pp. 2283
    • Verdon, G.1    Oh, S.2    Serio, R.N.3    Boudker, O.4
  • 73
    • 33750470835 scopus 로고    scopus 로고
    • Activation of a presynaptic glutamate transporter regulates synaptic transmission through electrical signaling
    • PID: 17041592
    • Veruki ML, Morkve SH, Hartveit E (2006) Activation of a presynaptic glutamate transporter regulates synaptic transmission through electrical signaling. Nat Neurosci 9:1388–1396
    • (2006) Nat Neurosci , vol.9 , pp. 1388-1396
    • Veruki, M.L.1    Morkve, S.H.2    Hartveit, E.3
  • 74
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport
    • PID: 7546750
    • Wadiche JI, Amara SG, Kavanaugh MP (1995) Ion fluxes associated with excitatory amino acid transport. Neuron 15:721–728
    • (1995) Neuron , vol.15 , pp. 721-728
    • Wadiche, J.I.1    Amara, S.G.2    Kavanaugh, M.P.3
  • 75
    • 0032189020 scopus 로고    scopus 로고
    • Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel
    • PID: 9742136
    • Wadiche JI, Kavanaugh MP (1998) Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel. J Neurosci 18:7650–7661
    • (1998) J Neurosci , vol.18 , pp. 7650-7661
    • Wadiche, J.I.1    Kavanaugh, M.P.2
  • 76
    • 0034967684 scopus 로고    scopus 로고
    • Early intermediates in the transport cycle of the neuronal excitatory amino acid carrier EAAC1
    • PID: 11382805
    • Watzke N, Bamberg E, Grewer C (2001) Early intermediates in the transport cycle of the neuronal excitatory amino acid carrier EAAC1. J Gen Physiol 117:547–562
    • (2001) J Gen Physiol , vol.117 , pp. 547-562
    • Watzke, N.1    Bamberg, E.2    Grewer, C.3
  • 77
    • 33750695604 scopus 로고    scopus 로고
    • The glutamate transporter EAAT5 works as a presynaptic receptor in mouse rod bipolar cells
    • PID: 16973698
    • Wersinger E, Schwab Y, Sahel JA, Rendon A, Pow DV, Picaud S, Roux MJ (2006) The glutamate transporter EAAT5 works as a presynaptic receptor in mouse rod bipolar cells. J Physiol 577:221–234
    • (2006) J Physiol , vol.577 , pp. 221-234
    • Wersinger, E.1    Schwab, Y.2    Sahel, J.A.3    Rendon, A.4    Pow, D.V.5    Picaud, S.6    Roux, M.J.7
  • 78
    • 84870203648 scopus 로고    scopus 로고
    • A point mutation associated with episodic ataxia 6 increases glutamate transporter anion currents
    • PID: 23107647
    • Winter N, Kovermann P, Fahlke C (2012) A point mutation associated with episodic ataxia 6 increases glutamate transporter anion currents. Brain 135:3416–3425. doi:10.1093/brain/aws255
    • (2012) Brain , vol.135 , pp. 3416-3425
    • Winter, N.1    Kovermann, P.2    Fahlke, C.3
  • 79
    • 0017619677 scopus 로고
    • Anion selectivity in biological systems
    • PID: 834775
    • Wright EM, Diamond JM (1977) Anion selectivity in biological systems. Physiol Rev 57:109–156
    • (1977) Physiol Rev , vol.57 , pp. 109-156
    • Wright, E.M.1    Diamond, J.M.2
  • 80
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • PID: 15483603
    • Yernool D, Boudker O, Jin Y, Gouaux E (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431:811–818
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.