메뉴 건너뛰기




Volumn 445, Issue 7126, 2007, Pages 387-393

Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSPORTER; ASPARTATE TRANSPORTER; ASPARTIC ACID; ASPARTIC ACID DERIVATIVE; DEXTRO THREO BETA BENZYLOXYASPARTATE; SODIUM; SODIUM ION; UNCLASSIFIED DRUG;

EID: 33846505059     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05455     Document Type: Article
Times cited : (418)

References (45)
  • 2
    • 0004068805 scopus 로고
    • Sinauer Associates, Sunderland, Massachusetts
    • Läuger, P. Electrogenic Ion Pumps (Sinauer Associates, Sunderland, Massachusetts, 1991).
    • (1991) Electrogenic Ion Pumps
    • Läuger, P.1
  • 3
    • 0141582541 scopus 로고    scopus 로고
    • Quick, M. W, ed, Wiley-Liss, Hoboken, New Jersey
    • Quick, M. W. (ed.) Transmembrane Transporters (Wiley-Liss, Hoboken, New Jersey, 2002).
    • (2002) Transmembrane Transporters
  • 4
    • 15744387867 scopus 로고    scopus 로고
    • Structural and mechanistic diversity of secondary transporters
    • Sobczak, I. & Lolkema, J. S. Structural and mechanistic diversity of secondary transporters. Curr. Opin. Microbiol. 8, 161-167 (2005).
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 161-167
    • Sobczak, I.1    Lolkema, J.S.2
  • 5
    • 1242295211 scopus 로고    scopus 로고
    • Synaptic uptake and beyond: The sodium- and chloride-dependent neurotransmitter transporter family SLC6
    • Chen, N. H., Reith, M. E. & Quick, M. W. Synaptic uptake and beyond: the sodium- and chloride-dependent neurotransmitter transporter family SLC6. Pflugers Arch. 447, 519-531 (2004).
    • (2004) Pflugers Arch , vol.447 , pp. 519-531
    • Chen, N.H.1    Reith, M.E.2    Quick, M.W.3
  • 6
    • 1242272759 scopus 로고    scopus 로고
    • The sodium/glucose cotransport family SLC5
    • Wright, E. M. & Turk, E. The sodium/glucose cotransport family SLC5. Pflugers Arch. 447, 510-518 (2004).
    • (2004) Pflugers Arch , vol.447 , pp. 510-518
    • Wright, E.M.1    Turk, E.2
  • 7
    • 0035342615 scopus 로고    scopus 로고
    • Sodium-substrate cotransport in bacteria
    • Wilson, T. H. & Ding, P. Z. Sodium-substrate cotransport in bacteria. Biochim. Biophys. Acta 1505, 121-130 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 121-130
    • Wilson, T.H.1    Ding, P.Z.2
  • 8
    • 17744363326 scopus 로고    scopus 로고
    • Electrogenic glutamate transporters in the CNS: Molecular mechanism, pre-steady-state kinetics, and their impact on synaptic signaling
    • Grewer, C. & Rauen, T. Electrogenic glutamate transporters in the CNS: molecular mechanism, pre-steady-state kinetics, and their impact on synaptic signaling. J. Membr. Biol. 203, 1-20 (2005).
    • (2005) J. Membr. Biol , vol.203 , pp. 1-20
    • Grewer, C.1    Rauen, T.2
  • 10
    • 0020448447 scopus 로고
    • Binding order of substrates to the sodium and potassium ion coupled L-glutamatic acid transporter from rat brain
    • Kanner, B. I. & Bendahan, A. Binding order of substrates to the sodium and potassium ion coupled L-glutamatic acid transporter from rat brain. Biochemistry 21, 6327-6330 (1982).
    • (1982) Biochemistry , vol.21 , pp. 6327-6330
    • Kanner, B.I.1    Bendahan, A.2
  • 11
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue, N. & Kavanaugh, M. P. Flux coupling in a neuronal glutamate transporter. Nature 383, 634-637 (1996).
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 13
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y. & Gouaux, E. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431, 811-818 (2004).
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 14
    • 24344507684 scopus 로고    scopus 로고
    • Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other
    • Grewer, C. et al. Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other. Biochemistry 44, 11913-11923 (2005).
    • (2005) Biochemistry , vol.44 , pp. 11913-11923
    • Grewer, C.1
  • 15
    • 14044263640 scopus 로고    scopus 로고
    • Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters
    • Koch, H. P. & Larsson, H. P. Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters. J. Neurosci. 25, 1730-1736 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 1730-1736
    • Koch, H.P.1    Larsson, H.P.2
  • 17
    • 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. Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. Neuron 21, 623-632 (1998).
    • (1998) Neuron , vol.21 , pp. 623-632
    • Grunewald, M.1    Bendahan, A.2    Kanner, B.I.3
  • 18
    • 0029913959 scopus 로고    scopus 로고
    • Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family
    • Slotboom, D. J., Lolkema, J. S. & Konings, W. N. Membrane topology of the C-terminal half of the neuronal, glial, and bacterial glutamate transporter family. J. Biol. Chem. 271, 31317-31321 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 31317-31321
    • Slotboom, D.J.1    Lolkema, J.S.2    Konings, W.N.3
  • 19
    • 0032434691 scopus 로고    scopus 로고
    • A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation
    • Seal, R. P. & Amara, S. G. A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation. Neuron 21, 1487-1498 (1998).
    • (1998) Neuron , vol.21 , pp. 1487-1498
    • Seal, R.P.1    Amara, S.G.2
  • 20
    • 0033431036 scopus 로고    scopus 로고
    • A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive reentrant loop
    • Slotboom, D. J., Sobczak, I., Konings, W. N. & Lolkema, J. S. A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive reentrant loop. Proc. Natl Acad. Sci. USA 96, 14282-14287 (1999).
    • (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
  • 21
    • 0034737622 scopus 로고    scopus 로고
    • The accessibility of a novel reentrant loop of the glutamate transporter GLT-1 is restricted by its substrate
    • Grunewald, M. & Kanner, B. I. The accessibility of a novel reentrant loop of the glutamate transporter GLT-1 is restricted by its substrate. J. Biol. Chem. 275, 9684-9689 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 9684-9689
    • Grunewald, M.1    Kanner, B.I.2
  • 22
    • 0035815643 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis reveals a highly amphipathic, pore-lining membrane-spanning helix in the glutamate transporter GltT
    • Slotboom, D. J., Konings, W. N. & Lolkema, J. S. Cysteine-scanning mutagenesis reveals a highly amphipathic, pore-lining membrane-spanning helix in the glutamate transporter GltT. J. Biol. Chem. 276, 10775-10781 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 10775-10781
    • Slotboom, D.J.1    Konings, W.N.2    Lolkema, J.S.3
  • 23
    • 0037135617 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis reveals a conformationally sensitive reentrant pore-loop in the glutamate transporter GLT-1
    • Grunewald, M., Menaker, D. & Kanner, B. I. Cysteine-scanning mutagenesis reveals a conformationally sensitive reentrant pore-loop in the glutamate transporter GLT-1. J. Biol. Chem. 277, 26074-26080 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 26074-26080
    • Grunewald, M.1    Menaker, D.2    Kanner, B.I.3
  • 24
    • 0031909675 scopus 로고    scopus 로고
    • DL-threo-β-benzyloxyaspartate, a potent blocker of excitatory amino acid transporters
    • Shimamoto, K. et al. DL-threo-β-benzyloxyaspartate, a potent blocker of excitatory amino acid transporters. Mol. Pharmacol. 53, 195-201 (1998).
    • (1998) Mol. Pharmacol , vol.53 , pp. 195-201
    • Shimamoto, K.1
  • 25
    • 0023074631 scopus 로고
    • Mechanism of transport and storage of neurotransmitters
    • Kanner, B. I. & Schuldiner, S. Mechanism of transport and storage of neurotransmitters. CRC Crit. Rev. Biochem. 22, 1-38 (1987).
    • (1987) CRC Crit. Rev. Biochem , vol.22 , pp. 1-38
    • Kanner, B.I.1    Schuldiner, S.2
  • 26
    • 0025052336 scopus 로고
    • The release and uptake of excitatory amino acids
    • Nicholls, D. & Attwell, D. The release and uptake of excitatory amino acids. Trends Pharmacol. Sci. 11, 462-468 (1990).
    • (1990) Trends Pharmacol. Sci , vol.11 , pp. 462-468
    • Nicholls, D.1    Attwell, D.2
  • 27
    • 0028031487 scopus 로고
    • Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex
    • Arriza, J. L. et al. Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. J. Neurosci. 14, 5559-5569 (1994).
    • (1994) J. Neurosci , vol.14 , pp. 5559-5569
    • Arriza, J.L.1
  • 28
    • 0035448934 scopus 로고    scopus 로고
    • Glutamate transporters combine transporter- and channel-like features
    • Slotboom, D. J., Konings, W. N. & Lolkema, J. S. Glutamate transporters combine transporter- and channel-like features. Trends Biochem. Sci. 26, 534-539 (2001).
    • (2001) Trends Biochem. Sci , vol.26 , pp. 534-539
    • Slotboom, D.J.1    Konings, W.N.2    Lolkema, J.S.3
  • 30
    • 13244295377 scopus 로고    scopus 로고
    • Sinorhizobium meliloti dctA mutants with partial ability to transport dicarboxylic acids
    • Yurgel, S. N. & Kahn, M. L. Sinorhizobium meliloti dctA mutants with partial ability to transport dicarboxylic acids. J. Bacteriol. 187, 1161-1172 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 1161-1172
    • Yurgel, S.N.1    Kahn, M.L.2
  • 31
    • 0027176433 scopus 로고
    • +/glutamate cotransporters
    • +/glutamate cotransporters. J. Biol. Chem. 268, 15351-15355 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 15351-15355
    • Shafqat, S.1
  • 32
    • 0027327563 scopus 로고
    • Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter family
    • Arriza, J. L. et al. Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter family. J. Biol. Chem. 268, 15329-15332 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 15329-15332
    • Arriza, J.L.1
  • 33
    • 0032436625 scopus 로고    scopus 로고
    • +-coupled serine transporter from Escherichia coli and characteristics of the transporter
    • +-coupled serine transporter from Escherichia coli and characteristics of the transporter. J. Bacteriol. 180, 6749-6752 (1998).
    • (1998) J. Bacteriol , vol.180 , pp. 6749-6752
    • Ogawa, W.1    Kim, Y.-M.2    Mizushima, T.3    Tsuchiya, T.4
  • 34
    • 0028911077 scopus 로고
    • Differential modulation of human glutamate transporter subtypes by arachidonic acid
    • Zerangue, N., Arriza, J. L., Amara, S. G. & Kavanaugh, M. P. Differential modulation of human glutamate transporter subtypes by arachidonic acid. J. Biol. Chem. 270, 6433-6435 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 6433-6435
    • Zerangue, N.1    Arriza, J.L.2    Amara, S.G.3    Kavanaugh, M.P.4
  • 35
    • 0018132541 scopus 로고
    • Active transport of L-glutamate by membrane vesicles isolated from rat brain
    • Kanner, B. I. & Sharon, I. Active transport of L-glutamate by membrane vesicles isolated from rat brain. Biochemistry 17, 3949-3953 (1978).
    • (1978) Biochemistry , vol.17 , pp. 3949-3953
    • Kanner, B.I.1    Sharon, I.2
  • 36
    • 24944545617 scopus 로고    scopus 로고
    • Lone pair effect in thallium(I) macrocyclic compounds
    • Mudring, A.-V. & Rieger, F. Lone pair effect in thallium(I) macrocyclic compounds. Inorg. Chem. 44, 6240-6243 (2005).
    • (2005) Inorg. Chem , vol.44 , pp. 6240-6243
    • Mudring, A.-V.1    Rieger, F.2
  • 37
    • 33744518437 scopus 로고    scopus 로고
    • + to the glutamate-free form and cycling of the glutamate carrier EAAC1
    • + to the glutamate-free form and cycling of the glutamate carrier EAAC1. J. Biol. Chem. 281, 10263-10272 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 10263-10272
    • Tao, Z.1    Zhang, Z.2    Grewer, C.3
  • 38
    • 0037055984 scopus 로고    scopus 로고
    • The dual-function glutamate transporters: Structure and molecular characterization of the substrate binding sites
    • Kanner, B. I. & Borre, L. The dual-function glutamate transporters: structure and molecular characterization of the substrate binding sites. Biochim. Biophys. Acta 1555, 92-95 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 92-95
    • Kanner, B.I.1    Borre, L.2
  • 39
    • 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. 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).
    • (1998) J. Biol. Chem , vol.273 , pp. 14231-14237
    • Zarbiv, R.1    Grunewald, M.2    Kavanaugh, M.P.3    Kanner, B.I.4
  • 40
    • 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. 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).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1710-1715
    • Zhang, Y.1    Kanner, B.I.2
  • 41
    • 0037040231 scopus 로고    scopus 로고
    • Proximity of two oppositely oriented reentrant loops in the glutamate transporter GLT-1 indentified by paired cysteine mutagenesis
    • Brocke, L., Bendahan, A., Grunewald, M. & Kanner, B. I. Proximity of two oppositely oriented reentrant loops in the glutamate transporter GLT-1 indentified by paired cysteine mutagenesis. J. Biol. Chem. 277, 3985-3992 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 3985-3992
    • Brocke, L.1    Bendahan, A.2    Grunewald, M.3    Kanner, B.I.4
  • 42
    • 0029869003 scopus 로고    scopus 로고
    • Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus
    • Gaillard, I., Slotboom, D. J., Knol, J., Lolkema, J. S. & Konings, W. N. Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus. Biochemistry 35, 6150-6156 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6150-6156
    • Gaillard, I.1    Slotboom, D.J.2    Knol, J.3    Lolkema, J.S.4    Konings, W.N.5
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0028103275 scopus 로고    scopus 로고
    • CCP4 Project. N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • CCP4 Project. N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
  • 45
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt, G. J. Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr. D 52, 842-857 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.