메뉴 건너뛰기




Volumn 99, Issue 1, 2006, Pages 20-28

The substrate specificity of a neuronal glutamate transporter is determined by the nature of the coupling ion

Author keywords

Coupling ions; Neuronal glutamate transporter; Radioactive uptake; Reconstitution; Substrate specificity; Transport currents

Indexed keywords

ASPARTIC ACID; DEXTRO ASPARTIC ACID; GLUTAMATE TRANSPORTER; GLUTAMATE TRANSPORTER EAAC1; GLUTAMIC ACID; ION; LITHIUM; RADIOACTIVE MATERIAL; SODIUM; UNCLASSIFIED DRUG;

EID: 33748713433     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2006.04003.x     Document Type: Article
Times cited : (26)

References (34)
  • 1
    • 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. and 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
  • 2
    • 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. and 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
  • 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. and Kanner B. I. (2000) Arginine 447 plays a pivotal role in substrate interactions in a neuronal glutamate transporter. J. Biol. Chem. 275, 37 436-37 442.
    • (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
    • 0036896927 scopus 로고    scopus 로고
    • Comparison of coupled and uncoupled currents during glutamate uptake by GLT-1 transporters
    • Bergles D. E., Tzingounis A. V. and Jahr C. E. (2002) Comparison of coupled and uncoupled currents during glutamate uptake by GLT-1 transporters. J. Neurosci. 22, 10 153-10 162.
    • (2002) J. Neurosci. , vol.22 , pp. 10153-10162
    • Bergles, D.E.1    Tzingounis, A.V.2    Jahr, C.E.3
  • 5
    • 0035798626 scopus 로고    scopus 로고
    • Coupled, but not uncoupled, fluxes in a neuronal glutamate transporter can be activated by lithium ions
    • Borre L. and Kanner B. I. (2001) Coupled, but not uncoupled, fluxes in a neuronal glutamate transporter can be activated by lithium ions. J. Biol. Chem. 276, 40 396-40 401.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40396-40401
    • Borre, L.1    Kanner, B.I.2
  • 6
    • 1642494714 scopus 로고    scopus 로고
    • Arginine 445 controls the coupling between glutamate and cations in the neuronal transporter EAAC-1
    • Borre L. and 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
  • 7
    • 0023260545 scopus 로고
    • Electrogenic glutamate uptake is a major current carrier in the membrane of axolotl retinal glial cells
    • Brew H. and 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
  • 8
    • 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. and 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
  • 9
    • 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. and 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
  • 10
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst T. R., Niles E. G., Studier F. W. and Moss B. (1986) Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl Acad. Sci. USA 83, 8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 11
    • 0029041792 scopus 로고
    • Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states
    • Grunewald M. and Kanner B. (1995) Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter- bound states. J. Biol. Chem. 270, 17 017-17 024.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17017-17024
    • Grunewald, M.1    Kanner, B.2
  • 12
    • 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. and 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
  • 13
    • 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. and 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
  • 14
    • 0026458124 scopus 로고
    • Primary structure and functional characterization of a high-affinity glutamate transporter
    • Kanai Y. and 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
  • 15
    • 0020448447 scopus 로고
    • Binding order of substrates to the sodium and potassium ion coupled L-glutamic acid transporter from rat brain
    • Kanner B. I. and 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
  • 16
    • 0018132541 scopus 로고
    • Active transport of L-glutamate by membrane vesicles isolated from rat brain
    • Kanner B. I. and 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
  • 17
    • 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. and 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
  • 18
    • 0026691409 scopus 로고
    • Expression of a cloned c-aminobutyric acid transporter in mammalian cells
    • Keynan S., Suh Y. J., Kanner B. I. and Rudnick G. (1992) Expression of a cloned c-aminobutyric acid transporter in mammalian cells. Biochemistry 31, 1974-1979.
    • (1992) Biochemistry , vol.31 , pp. 1974-1979
    • Keynan, S.1    Suh, Y.J.2    Kanner, B.I.3    Rudnick, G.4
  • 22
    • 0025691629 scopus 로고
    • Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain
    • Pines G. and Kanner B. I. (1990) Counterflow of L-glutamate in plasma membrane vesicles and reconstituted preparations from rat brain. Biochemistry 29, 11 209-11 214.
    • (1990) Biochemistry , vol.29 , pp. 11209-11214
    • Pines, G.1    Kanner, B.I.2
  • 24
    • 1842585550 scopus 로고    scopus 로고
    • Characterization of novel L-threo-β-benzyloxyaspartate derivatives, potent blockers of the glutamate transporters
    • Shimamoto K., Sakai R., Takaoka K., Yumoto N., Nakajima T., Amara S. G. and Shigeri Y. (2004) Characterization of novel L-threo-β- benzyloxyaspartate derivatives, potent blockers of the glutamate transporters. Mol. Pharmacol. 65, 1008-1015.
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1008-1015
    • Shimamoto, K.1    Sakai, R.2    Takaoka, K.3    Yumoto, N.4    Nakajima, T.5    Amara, S.G.6    Shigeri, Y.7
  • 25
    • 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. and 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, 14 282-14 287.
    • (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
  • 26
    • 0027182377 scopus 로고
    • Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites
    • Toney M. D., Hohenester E., Cowan S. W. and Jansonius J. N. (1993) Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science 261, 756-759.
    • (1993) Science , vol.261 , pp. 756-759
    • Toney, M.D.1    Hohenester, E.2    Cowan, S.W.3    Jansonius, J.N.4
  • 27
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport
    • Wadiche J. I., Amara S. G. and Kavanaugh M. P. (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
  • 28
    • 0034967684 scopus 로고    scopus 로고
    • Early intermediates in the transport cycle of the neuronal excitatory amino acid carrier EAAC1
    • Watzke N., Bamberg E. and 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
  • 30
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool D., Boudker O., Jin Y. and 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
  • 31
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue N. and Kavanaugh M. P. (1996a) 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
  • 32
    • 0029891464 scopus 로고    scopus 로고
    • Interaction of L-cysteine with a human excitatory amino acid transporter
    • Zerangue N. and Kavanaugh M. P. (1996b) Interaction of L-cysteine with a human excitatory amino acid transporter. J. Physiol. 493, 419-423.
    • (1996) J. Physiol. , vol.493 , pp. 419-423
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 33
    • 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. and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.