메뉴 건너뛰기




Volumn 213, Issue 2, 2006, Pages 89-100

Structure and function of sodium-coupled GABA and glutamate transporters

Author keywords

Function; GABA; Glutamate; Structure; Transporter

Indexed keywords

4 AMINOBUTYRIC ACID CARRIER; GLUTAMATE TRANSPORTER;

EID: 34247203194     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-006-0877-5     Document Type: Review
Times cited : (87)

References (83)
  • 1
    • 0030932152 scopus 로고    scopus 로고
    • Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance
    • Arriza, J.L., Eliasof, S., Kavanaugh, M.P., Amara, S.G. 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
  • 2
    • 0028031487 scopus 로고
    • Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex
    • Arriza, J.L., Fairman, W.A., Wadiche, J.I., Murdoch, G.H., Kavanaugh, M.P., Amara, S.G. 1994. Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. J. Neurosci. 14:5559-5569
    • (1994) J. Neurosci , vol.14 , pp. 5559-5569
    • Arriza, J.L.1    Fairman, W.A.2    Wadiche, J.I.3    Murdoch, G.H.4    Kavanaugh, M.P.5    Amara, S.G.6
  • 3
    • 0034529012 scopus 로고    scopus 로고
    • Arginine 447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter
    • Bendahan, A., Armon, A., Madani, N., Kavanaugh, M.P., Kanner, B.I. 2000. Arginine 447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter. J. Biol. Chem. 275:37436-37442
    • (2000) J. Biol. Chem , vol.275 , pp. 37436-37442
    • Bendahan, A.1    Armon, A.2    Madani, N.3    Kavanaugh, M.P.4    Kanner, B.I.5
  • 4
    • 0034602317 scopus 로고    scopus 로고
    • Mutation of arginine 44 of GAT-1, a (Na(+) + Cl(-))-coupled gamma-aminobutyric acid transporter from rat brain, impairs net flux but not exchange
    • Bennett, E.R., Su, H., Kanner, B.I. 2000. Mutation of arginine 44 of GAT-1, a (Na(+) + Cl(-))-coupled gamma-aminobutyric acid transporter from rat brain, impairs net flux but not exchange. J. Biol. Chem. 275:34106-34113
    • (2000) J. Biol. Chem , vol.275 , pp. 34106-34113
    • Bennett, E.R.1    Su, H.2    Kanner, B.I.3
  • 5
    • 0029973191 scopus 로고    scopus 로고
    • Anion conductance behavior of the glutamate uptake carrier in salamander retinal glial cells
    • Billups, B., Rossi, D., Attwell, D. 1996. Anion conductance behavior of the glutamate uptake carrier in salamander retinal glial cells. J. Neurosci. 16:6722-6731
    • (1996) J. Neurosci , vol.16 , pp. 6722-6731
    • Billups, B.1    Rossi, D.2    Attwell, D.3
  • 6
    • 0030921440 scopus 로고    scopus 로고
    • Tyrosine 140 of the gammaaminobutyric acid transporter GAT-1 plays a critical role in neurotransmitter recognition
    • Bismuth, Y., Kavanaugh, M.P., Kanner, B.I. 1997. Tyrosine 140 of the gammaaminobutyric acid transporter GAT-1 plays a critical role in neurotransmitter recognition. J. Biol. Chem. 272:16096-16102
    • (1997) J. Biol. Chem , vol.272 , pp. 16096-16102
    • Bismuth, Y.1    Kavanaugh, M.P.2    Kanner, B.I.3
  • 7
    • 0035798626 scopus 로고    scopus 로고
    • Coupled, but not uncoupled, fluxes in a neuronal glutamate transporter can be activated by lithium ions
    • Borre, L., Kanner, B.I. 2001. Coupled, but not uncoupled, fluxes in a neuronal glutamate transporter can be activated by lithium ions. J. Biol. Chem. 276:40396-40401
    • (2001) J. Biol. Chem , vol.276 , pp. 40396-40401
    • Borre, L.1    Kanner, B.I.2
  • 8
    • 1642494714 scopus 로고    scopus 로고
    • Arginine 445 controls the coupling between glutamate and cations in the neuronal transporter EAAC-1
    • Borre, L., Kanner, B.I. 2004. Arginine 445 controls the coupling between glutamate and cations in the neuronal 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
  • 9
    • 0037134479 scopus 로고    scopus 로고
    • Dynamic equilibrium between coupled and uncoupled modes of a neuronal glutamate transporter
    • Borre, L., Kavanaugh, M.P., Kanner, B.I. 2002. Dynamic equilibrium between coupled and uncoupled modes of a neuronal glutamate transporter. J. Biol. Chem. 277:13501-13507
    • (2002) J. Biol. Chem , vol.277 , pp. 13501-13507
    • Borre, L.1    Kavanaugh, M.P.2    Kanner, B.I.3
  • 10
    • 0023260545 scopus 로고
    • Electrogenic glutamate uptake is a major current carrier in the membrane of axolotl retinal glial cells
    • Brew, H., Attwell, D. 1987. Electrogenic glutamate uptake is a major current carrier in the membrane of axolotl retinal glial cells. Nature 327:707-709
    • (1987) Nature , vol.327 , pp. 707-709
    • Brew, H.1    Attwell, D.2
  • 11
    • 0037040231 scopus 로고    scopus 로고
    • Proximity of two oppositely oriented re-entrant loops in the glutamate transporter GLT-1 identified by paired cysteine mutagenesis
    • Brocke, L., Bendahan, A., Grunewald, M., Kanner, B.I. 2002. Proximity of two oppositely oriented re-entrant loops in the glutamate transporter GLT-1 identified by paired cysteine mutagenesis. J. Biol. Chem. 277:3985-3992
    • (2002) J. Biol. Chem , vol.277 , pp. 3985-3992
    • Brocke, L.1    Bendahan, A.2    Grunewald, M.3    Kanner, B.I.4
  • 12
    • 0032524637 scopus 로고    scopus 로고
    • Determination of external loop topology in the serotonin transporter by site-directed chemical labeling
    • Chen, J.G., Liu-Chen, S., Rudnick, G. 1998. Determination of external loop topology in the serotonin transporter by site-directed chemical labeling. J. Biol. Chem. 273:12675-12681
    • (1998) J. Biol. Chem , vol.273 , pp. 12675-12681
    • Chen, J.G.1    Liu-Chen, S.2    Rudnick, G.3
  • 13
    • 0029864153 scopus 로고    scopus 로고
    • Retinal glial cell glutamate transporter is coupled to an anionic conductance
    • Eliasof, S., Jahr, C.E. 1996. Retinal glial cell glutamate transporter is coupled to an anionic conductance. Proc. Natl. Acad. Sci. USA 93:4153-4158
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4153-4158
    • Eliasof, S.1    Jahr, C.E.2
  • 14
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • Fairman, W.A., Vandenberg, R.J., Arriza, J.L., Kavanaugh, M.P., Amara, S.G. 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
  • 15
    • 0030071106 scopus 로고    scopus 로고
    • Hyperlocomotion and indifference to cocaine and amphetamine in mice lacking the dopamine transporter
    • Giros, B., Jaber, M., Jones, S.R., Wightman, R.M., Caron, M.G. 1996. Hyperlocomotion and indifference to cocaine and amphetamine in mice lacking the dopamine transporter. Nature 379:606-612
    • (1996) Nature , vol.379 , pp. 606-612
    • Giros, B.1    Jaber, M.2    Jones, S.R.3    Wightman, R.M.4    Caron, M.G.5
  • 16
    • 0033551736 scopus 로고    scopus 로고
    • The reactivity of the gamma-aminobutyric acid transporter GAT-1 toward sulfhydryl reagents is conformationally sensitive. Identification of a major target residue
    • Golovanevsky, V., Kanner, B.I. 1999. The reactivity of the gamma-aminobutyric acid transporter GAT-1 toward sulfhydryl reagents is conformationally sensitive. Identification of a major target residue. J. Biol. Chem. 274:23020-23026
    • (1999) J. Biol. Chem , vol.274 , pp. 23020-23026
    • Golovanevsky, V.1    Kanner, B.I.2
  • 17
    • 0037462748 scopus 로고    scopus 로고
    • Is the glutamate residue Glu-373 the proton acceptor of the excitatory amino acid carrier 1?
    • Grewer, C., Watzke, N., Rauen, T., Bicho, A. 2003. Is the glutamate residue Glu-373 the proton acceptor of the excitatory amino acid carrier 1? J. Biol. Chem. 278:2585-2592
    • (2003) J. Biol. Chem , vol.278 , pp. 2585-2592
    • Grewer, C.1    Watzke, N.2    Rauen, T.3    Bicho, A.4
  • 18
    • 0032169137 scopus 로고    scopus 로고
    • Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology
    • Grunewald, M., Bendahan, A., Kanner, B.I. 1998. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Neuron. 21:623-632
    • (1998) Neuron , vol.21 , pp. 623-632
    • Grunewald, M.1    Bendahan, A.2    Kanner, B.I.3
  • 19
    • 0029041792 scopus 로고
    • Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states
    • Grunewald, M., Kanner, B. 1995. Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states. J. Biol. Chem. 270:17017-17024
    • (1995) J. Biol. Chem , vol.270 , pp. 17017-17024
    • Grunewald, M.1    Kanner, B.2
  • 20
    • 0034737622 scopus 로고    scopus 로고
    • The accessibility of a novel re-entrant loop of the glutamate transporter GLT-1 is restricted by its substrate
    • Grunewald, M., Kanner, B.I. 2000. The accessibility of a novel re-entrant loop of the glutamate transporter GLT-1 is restricted by its substrate. J. Biol. Chem. 275:9684-9689
    • (2000) J. Biol. Chem , vol.275 , pp. 9684-9689
    • Grunewald, M.1    Kanner, B.I.2
  • 21
    • 0037135617 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis reveals a conformationally sensitive re-entrant pore-loop in the glutamate transporter GLT-1
    • Grunewald, M., Menaker, D., Kanner, B.I. 2002. Cysteine-scanning mutagenesis reveals a conformationally sensitive re-entrant pore-loop in the glutamate transporter GLT-1. J. Biol. Chem. 277:26074-26080
    • (2002) J. Biol. Chem , vol.277 , pp. 26074-26080
    • Grunewald, M.1    Menaker, D.2    Kanner, B.I.3
  • 23
    • 0032885746 scopus 로고    scopus 로고
    • GAT1 (GABA:Na+:Cl-) cotransport function. Database reconstruction with an alternating access model
    • Hilgemann, D.W., Lu, C.C. 1999. GAT1 (GABA:Na+:Cl-) cotransport function. Database reconstruction with an alternating access model. J. Gen. Physiol. 114:459-475
    • (1999) J. Gen. Physiol , vol.114 , pp. 459-475
    • Hilgemann, D.W.1    Lu, C.C.2
  • 25
    • 0026458124 scopus 로고
    • Primary structure and functional characterization of a high-affinity glutamate transporter
    • Kanai, Y., Hediger, M.A. 1992. Primary structure and functional characterization of a high-affinity glutamate transporter. Nature 360:467-471
    • (1992) Nature , vol.360 , pp. 467-471
    • Kanai, Y.1    Hediger, M.A.2
  • 26
    • 0018138165 scopus 로고
    • Active transport of gamma-aminobutyric acid by membrane vesicles isolated from rat brain
    • Kanner, B.I. 1978. Active transport of gamma-aminobutyric acid by membrane vesicles isolated from rat brain. Biochemistry 17:1207-1211
    • (1978) Biochemistry , vol.17 , pp. 1207-1211
    • Kanner, B.I.1
  • 27
    • 0021067890 scopus 로고
    • Bioenergetics of neurotransmitter transport
    • Kanner, B.I. 1983. Bioenergetics of neurotransmitter transport. Biochim. Biophys. Acta. 726:293-316
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 293-316
    • Kanner, B.I.1
  • 28
    • 0024343868 scopus 로고
    • Ion-coupled neurotransmitter transport
    • Kanner, B.I. 1989. Ion-coupled neurotransmitter transport. Curr. Opin. Cell Biol. 1:735-738
    • (1989) Curr. Opin. Cell Biol , vol.1 , pp. 735-738
    • Kanner, B.I.1
  • 29
    • 0037423375 scopus 로고    scopus 로고
    • Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modes
    • Kanner, B.I. 2003. Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modes. J. Biol. Chem. 278:3705-3712
    • (2003) J. Biol. Chem , vol.278 , pp. 3705-3712
    • Kanner, B.I.1
  • 30
    • 24644519925 scopus 로고    scopus 로고
    • Molecular physiology: Intimate contact enables transport
    • Kanner, B.I. 2005. Molecular physiology: intimate contact enables transport. Nature 437:203-205
    • (2005) Nature , vol.437 , pp. 203-205
    • Kanner, B.I.1
  • 31
    • 0020448447 scopus 로고
    • Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain
    • Kanner, B.I., Bendahan, A. 1982. Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain. Biochemistry 21:6327-6330
    • (1982) Biochemistry , vol.21 , pp. 6327-6330
    • Kanner, B.I.1    Bendahan, A.2
  • 32
    • 0037055984 scopus 로고    scopus 로고
    • The dual-function glutamate transporters: Structure and molecular characterisation of the substrate-binding sites
    • Kanner, B.I., Borre, L. 2002. The dual-function glutamate transporters: structure and molecular characterisation of the substrate-binding sites. Biochim. Biophys. Acta. 1555:92-95
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 92-95
    • Kanner, B.I.1    Borre, L.2
  • 33
    • 0019950576 scopus 로고
    • Efflux of L-glutamate by synaptic plasma membrane vesicles isolated from rat brain
    • Kanner, B.I., Marva, E. 1982. Efflux of L-glutamate by synaptic plasma membrane vesicles isolated from rat brain. Biochemistry 21:3143-3147
    • (1982) Biochemistry , vol.21 , pp. 3143-3147
    • Kanner, B.I.1    Marva, E.2
  • 34
    • 0023074631 scopus 로고
    • Mechanism of transport and storage of neurotransmitters
    • Kanner, B.I., Schuldiner, S. 1987. Mechanism of transport and storage of neurotransmitters. CRC Crit. Rev. Biochem. 22:1-38
    • (1987) CRC Crit. Rev. Biochem , vol.22 , pp. 1-38
    • Kanner, B.I.1    Schuldiner, S.2
  • 35
    • 0018132541 scopus 로고
    • Active transport of L-glutamate by membrane vesicles isolated from rat brain
    • Kanner, B.I., Sharon, I. 1978. Active transport of L-glutamate by membrane vesicles isolated from rat brain. Biochemistry 17:3949-3953
    • (1978) Biochemistry , vol.17 , pp. 3949-3953
    • Kanner, B.I.1    Sharon, I.2
  • 36
    • 0026595365 scopus 로고
    • Electrogenic uptake of gamma-aminobutyric acid by a cloned transporter expressed in Xenopus oocytes
    • Kavanaugh, M.P., Arriza, J.L., North, R.A., Amara, S.G. 1992. Electrogenic uptake of gamma-aminobutyric acid by a cloned transporter expressed in Xenopus oocytes. J. Biol. Chem. 267:22007-22009
    • (1992) J. Biol. Chem , vol.267 , pp. 22007-22009
    • Kavanaugh, M.P.1    Arriza, J.L.2    North, R.A.3    Amara, S.G.4
  • 37
    • 0031028206 scopus 로고    scopus 로고
    • Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange
    • Kavanaugh, M.P., Bendahan, A., Zerangue, N., Zhang, Y., Kanner, B.I. 1997. Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange. J. Biol. Chem. 272:1703-1708
    • (1997) J. Biol. Chem , vol.272 , pp. 1703-1708
    • Kavanaugh, M.P.1    Bendahan, A.2    Zerangue, N.3    Zhang, Y.4    Kanner, B.I.5
  • 38
    • 0023831030 scopus 로고
    • gamma-Aminobutyric acid transport in reconstituted preparations from rat brain: Coupled sodium and chloride fluxes
    • Keynan, S., Kanner, B.I. 1988. gamma-Aminobutyric acid transport in reconstituted preparations from rat brain: coupled sodium and chloride fluxes. Biochemistry 27:12-17
    • (1988) Biochemistry , vol.27 , pp. 12-17
    • Keynan, S.1    Kanner, B.I.2
  • 39
    • 27844506567 scopus 로고    scopus 로고
    • Indentification and selective inhibition of the channel mode of the neuronal GABA transporter 1
    • Krause, S., Schwarz, W. 2005. Indentification and selective inhibition of the channel mode of the neuronal GABA transporter 1. Mol. Pharmacol. 68:1728-1735
    • (2005) Mol. Pharmacol , vol.68 , pp. 1728-1735
    • Krause, S.1    Schwarz, W.2
  • 42
    • 0032886824 scopus 로고    scopus 로고
    • -) cotransport function. Kinetic studies in giant Xenopus oocyte membrane patches
    • -) cotransport function. Kinetic studies in giant Xenopus oocyte membrane patches. J. Gen. Physiol. 114:445-457
    • (1999) J. Gen. Physiol , vol.114 , pp. 445-457
    • Lu, C.C.1    Hilgemann, D.W.2
  • 43
    • 0032888516 scopus 로고    scopus 로고
    • -) cotransport function. Steady state studies in giant Xenopus oocyte membrane patches
    • -) cotransport function. Steady state studies in giant Xenopus oocyte membrane patches. J. Gen. Physiol. 114:429-444
    • (1999) J. Gen. Physiol , vol.114 , pp. 429-444
    • Lu, C.C.1    Hilgemann, D.W.2
  • 44
    • 0027214169 scopus 로고
    • The substrates of a sodium- and chloride-coupled gamma-aminobutyric acid transporter protect multiple sites throughout the protein against proteolytic cleavage
    • Mabjeesh, N.J., Kanner, B.I. 1993. The substrates of a sodium- and chloride-coupled gamma-aminobutyric acid transporter protect multiple sites throughout the protein against proteolytic cleavage. Biochemistry 32:8540-8546
    • (1993) Biochemistry , vol.32 , pp. 8540-8546
    • Mabjeesh, N.J.1    Kanner, B.I.2
  • 45
    • 0035798631 scopus 로고    scopus 로고
    • Engineered Zn(2+) switches in the gamma-aminobutyric acid (GABA) transporter-1. Differential effects on GABA uptake and currents
    • MacAulay, N., Bendahan, A., Loland, C.J., Zeuthen, T., Kanner, B.I., Gether, U. 2001. Engineered Zn(2+) switches in the gamma-aminobutyric acid (GABA) transporter-1. Differential effects on GABA uptake and currents. J. Biol. Chem. 276:40476-40485
    • (2001) J. Biol. Chem , vol.276 , pp. 40476-40485
    • MacAulay, N.1    Bendahan, A.2    Loland, C.J.3    Zeuthen, T.4    Kanner, B.I.5    Gether, U.6
  • 46
    • 0037107410 scopus 로고    scopus 로고
    • Conformational basis for the Li(+) induced leak current in the rat gamma-aminobutyric acid (GABA) transporter
    • MacAulay, N., Zeuthen, T., Gether, U. 2002. Conformational basis for the Li(+) induced leak current in the rat gamma-aminobutyric acid (GABA) transporter. J. Physiol. 544:447-458
    • (2002) J. Physiol , vol.544 , pp. 447-458
    • MacAulay, N.1    Zeuthen, T.2    Gether, U.3
  • 49
    • 0027537292 scopus 로고
    • Steady states, charge movements, and rates for a cloned GABA transporter expressed in Xenopus oocytes
    • Mager, S., Naeve, J., Quick, M., Labarca, C., Davidson, N., Lester, H.A. 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
  • 50
    • 2442640243 scopus 로고    scopus 로고
    • Transmembrane domains I and II of the gamma aminobutyric acid transporter GAT-4 contain molecular determinants of substrate specificity
    • Melamed, N., Kanner, B.I. 2004. Transmembrane domains I and II of the gamma aminobutyric acid transporter GAT-4 contain molecular determinants of substrate specificity. Mol. Pharmacol. 65:1452-1461
    • (2004) Mol. Pharmacol , vol.65 , pp. 1452-1461
    • Melamed, N.1    Kanner, B.I.2
  • 51
    • 33748713433 scopus 로고    scopus 로고
    • The substrate specificity of a neuronal glutamate transporter is determined by the nature of the coupling ion
    • Menaker, D., Bendahan, A., Kanner, B.I. 2006. The substrate specificity of a neuronal glutamate transporter is determined by the nature of the coupling ion. J. Neurochem. 99:20-28
    • (2006) J. Neurochem , vol.99 , pp. 20-28
    • Menaker, D.1    Bendahan, A.2    Kanner, B.I.3
  • 52
    • 0031753789 scopus 로고    scopus 로고
    • - neurotransmitter transporters
    • - neurotransmitter transporters. J. Neurochem. 71:1785-1803
    • (1998) J. Neurochem , vol.71 , pp. 1785-1803
    • Nelson, N.1
  • 53
    • 0018565377 scopus 로고
    • Coupling between platelet 5-hydroxytryptamine and potassium transport
    • Nelson, P.J., Rudnick, G. 1979. Coupling between platelet 5-hydroxytryptamine and potassium transport. J. Biol. Chem. 254:10084-10089
    • (1979) J. Biol. Chem , vol.254 , pp. 10084-10089
    • Nelson, P.J.1    Rudnick, G.2
  • 55
    • 0027532379 scopus 로고
    • Only one of the charged amino acids located in the transmembrane alpha-helices of the gamma-aminobutyric acid transporter (subtype A) is essential for its activity
    • Pantanowitz, S., Bendahan, A., Kanner, B.I. 1993. Only one of the charged amino acids located in the transmembrane alpha-helices of the gamma-aminobutyric acid transporter (subtype A) is essential for its activity. J. Biol. Chem. 268:3222-3225
    • (1993) J. Biol. Chem , vol.268 , pp. 3222-3225
    • Pantanowitz, S.1    Bendahan, A.2    Kanner, B.I.3
  • 57
    • 0025691629 scopus 로고
    • Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain
    • Pines, G., Kanner, B.I. 1990. Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain. Biochemistry 29:11209-14
    • (1990) Biochemistry , vol.29 , pp. 11209-11214
    • Pines, G.1    Kanner, B.I.2
  • 58
    • 0023002440 scopus 로고
    • Purification and identification of the functional sodium- and chloride-coupled gamma-aminobutyric acid transport glycoprotein from rat brain
    • Radian, R., Bendahan, A., Kanner, B.I. 1986. Purification and identification of the functional sodium- and chloride-coupled gamma-aminobutyric acid transport glycoprotein from rat brain. J. Biol. Chem. 261:15437-15441
    • (1986) J. Biol. Chem , vol.261 , pp. 15437-15441
    • Radian, R.1    Bendahan, A.2    Kanner, B.I.3
  • 59
    • 33748765517 scopus 로고    scopus 로고
    • Multiple consequences of mutating two conserved Beta-bridge forming residues in the translocation cycle of a neuronal glutamate transporter
    • Rosental, N., Bendahan, A., Kanner, B.I. 2006. Multiple consequences of mutating two conserved Beta-bridge forming residues in the translocation cycle of a neuronal glutamate transporter. J. Biol. Chem. 281: 27905-27918
    • (2006) J. Biol. Chem , vol.281 , pp. 27905-27918
    • Rosental, N.1    Bendahan, A.2    Kanner, B.I.3
  • 60
    • 2442693929 scopus 로고    scopus 로고
    • The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway
    • Ryan, R.M., Mitrovic, A.D., Vandenberg, R.J. 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
  • 61
    • 0037134466 scopus 로고    scopus 로고
    • Distinct conformational states mediate the transport and anion channel properties of the glutamate transporter EAAT-1
    • Ryan, R.M., Vandenberg, R.J. 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
  • 62
    • 0035909950 scopus 로고    scopus 로고
    • Sulfhydryl modification of V449C in the glutamate transporter EAAT1 abolishes substrate transport but not the substrate-gated anion conductance
    • Seal, R.P., Shigeri, Y., Eliasof, S., Leighton, B.H., Amara, S.G. 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
  • 63
    • 26944479295 scopus 로고    scopus 로고
    • Sulfhydryl modification of cysteine mutants of a neuronal glutamate transporter reveals an inverse relationship between sodium dependent conformational changes and the glutamate-gated anion conductance
    • Shachnai, L., Shimamoto, K., Kanner, B.I. 2005. Sulfhydryl modification of cysteine mutants of a neuronal glutamate transporter reveals an inverse relationship between sodium dependent conformational changes and the glutamate-gated anion conductance. Neuropharmacology 49:862-871
    • (2005) Neuropharmacology , vol.49 , pp. 862-871
    • Shachnai, L.1    Shimamoto, K.2    Kanner, B.I.3
  • 64
    • 0033431036 scopus 로고    scopus 로고
    • A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive re-entrant loop
    • Slotboom, D.J., Sobczak, I., Konings, W.N., Lolkema, J.S. 1999. A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive re-entrant loop. Proc. Natl. Acad. Sci. USA 96:14282-14287
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14282-14287
    • Slotboom, D.J.1    Sobczak, I.2    Konings, W.N.3    Lolkema, J.S.4
  • 65
    • 0026489330 scopus 로고
    • Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain
    • Storck, T., Schulte, S., Hofmann, K., Stoffel, W. 1992. Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain. Proc. Natl. Acad. Sci. USA 89:10955-10959
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10955-10959
    • Storck, T.1    Schulte, S.2    Hofmann, K.3    Stoffel, W.4
  • 66
    • 0025251185 scopus 로고
    • Non-vesicular release of glutamate from glial cells by reversed electrogenic glutamate uptake
    • Szatkowski, M., Barbour, B., Attwell, D. 1990. Non-vesicular release of glutamate from glial cells by reversed electrogenic glutamate uptake. Nature 348:443-446
    • (1990) Nature , vol.348 , pp. 443-446
    • Szatkowski, M.1    Barbour, B.2    Attwell, D.3
  • 68
    • 33744518437 scopus 로고    scopus 로고
    • + to the glutamate-free form and cycling of the glutamate transporter EAAC1
    • + 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
  • 69
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., Ogawa, H. 2000. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405:647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 70
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport
    • Wadiche, J.I., Amara, S.G., Kavanaugh, M.P. 1995a. 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
  • 72
    • 0035936565 scopus 로고    scopus 로고
    • Engineering conformational flexibility in the lactose permease of Escherichia coli: Use of glycine-scanning mutagenesis to rescue mutant Glu325 → Asp
    • Weinglass, A.B., Smirnova, I.N., Kaback, H.R. 2001. Engineering conformational flexibility in the lactose permease of Escherichia coli: use of glycine-scanning mutagenesis to rescue mutant Glu325 → Asp. Biochemistry 40:769-776
    • (2001) Biochemistry , vol.40 , pp. 769-776
    • Weinglass, A.B.1    Smirnova, I.N.2    Kaback, H.R.3
  • 74
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • 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
  • 75
    • 0032486463 scopus 로고    scopus 로고
    • Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue
    • Zarbiv, R., Grunewald, M., Kavanaugh, M.P., Kanner, B.I. 1998. Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue. J. Biol. Chem. 273:14231-14237
    • (1998) J. Biol. Chem , vol.273 , pp. 14231-14237
    • Zarbiv, R.1    Grunewald, M.2    Kavanaugh, M.P.3    Kanner, B.I.4
  • 76
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue, N., Kavanaugh, M.P. 1996. Flux coupling in a neuronal glutamate transporter. Nature 383:634-637
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 78
    • 0033573907 scopus 로고    scopus 로고
    • Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitter
    • Zhang, Y., Kanner, B.I. 1999. Two serine residues of the glutamate transporter GLT-1 are crucial for coupling the fluxes of sodium and the neurotransmitter. Proc. Natl. Acad. Sci. USA 96:1710-1715
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1710-1715
    • Zhang, Y.1    Kanner, B.I.2
  • 79
    • 1842791407 scopus 로고    scopus 로고
    • The aqueous accessibility in the external half of transmembrane domain I of the GABA transporter GAT-1 is modulated by its ligands
    • Zhou, Y., Bennett, E.R., Kanner, B.I. 2004. The aqueous accessibility in the external half of transmembrane domain I of the GABA transporter GAT-1 is modulated by its ligands. J. Biol. Chem. 279:13800-13808
    • (2004) J. Biol. Chem , vol.279 , pp. 13800-13808
    • Zhou, Y.1    Bennett, E.R.2    Kanner, B.I.3
  • 80
    • 20144378948 scopus 로고    scopus 로고
    • Transporter-associated currents in the gamma aminobutyric acid transporter GAT-1 are conditionally impaired by mutations of a conserved glycine residue
    • Zhou, Y., Kanner, B.I. 2005. Transporter-associated currents in the gamma aminobutyric acid transporter GAT-1 are conditionally impaired by mutations of a conserved glycine residue. J. Biol. Chem. 280:20316-20324
    • (2005) J. Biol. Chem , vol.280 , pp. 20316-20324
    • Zhou, Y.1    Kanner, B.I.2
  • 81
    • 33746839659 scopus 로고    scopus 로고
    • Identification of a lithium interaction site in the GABA transporter GAT-1
    • Zhou, Y., Zomot, E., Kanner, B.I. 2006. Identification of a lithium interaction site in the GABA transporter GAT-1. J. Biol. Chem. 281: 22092-22099
    • (2006) J. Biol. Chem , vol.281 , pp. 22092-22099
    • Zhou, Y.1    Zomot, E.2    Kanner, B.I.3
  • 82
    • 0242353345 scopus 로고    scopus 로고
    • The interaction of the gamma-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV
    • Zomot, E., Kanner, B.I. 2003. The interaction of the gamma-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV. J. Biol. Chem. 278:42950-42958
    • (2003) J. Biol. Chem , vol.278 , pp. 42950-42958
    • Zomot, E.1    Kanner, B.I.2
  • 83
    • 21844468766 scopus 로고    scopus 로고
    • Proximity of transmembrane domains 1 and 3 of the gamma-aminobutyric acid transporter GAT-1 inferred from paired cysteine mutagenesis
    • Zomot, E., Zhou, Y., Kanner, B.I. 2005. Proximity of transmembrane domains 1 and 3 of the gamma-aminobutyric acid transporter GAT-1 inferred from paired cysteine mutagenesis. J. Biol. Chem. 280:25512-25516
    • (2005) J. Biol. Chem , vol.280 , pp. 25512-25516
    • Zomot, E.1    Zhou, Y.2    Kanner, B.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.