메뉴 건너뛰기




Volumn 108, Issue 37, 2011, Pages 15141-15146

Large collective motions regulate the functional properties of glutamate transporter trimers

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; EXCITATORY AMINO ACID TRANSPORTER 1; GLUTAMATE TRANSPORTER; SHORT HAIRPIN RNA;

EID: 80053084303     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1112216108     Document Type: Article
Times cited : (52)

References (35)
  • 1
    • 34249935610 scopus 로고    scopus 로고
    • Glutamate and monoamine transporters: new visions of form and function
    • DOI 10.1016/j.conb.2007.05.002, PII S0959438807000682, Signalling mechanisms Edited by Stuart Cull-Candy and Rudiger Klein
    • Torres GE, Amara SG (2007) Glutamate and monoamine transporters: New visions of form and function. Curr Opin Neurobiol 17:304-312. (Pubitemid 46880333)
    • (2007) Current Opinion in Neurobiology , vol.17 , Issue.3 , pp. 304-312
    • Torres, G.E.1    Amara, S.G.2
  • 2
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • DOI 10.1038/383634a0
    • Zerangue N, Kavanaugh MP (1996) Flux coupling in a neuronal glutamate transporter. Nature 383:634-637. (Pubitemid 26347587)
    • (1996) Nature , vol.383 , Issue.6601 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 3
    • 0032488807 scopus 로고    scopus 로고
    • Inducible expression of the GLT-1 glutamate transporter in a CHO cell line selected for low endogenous glutamate uptake
    • DOI 10.1016/S0014-5793(98)00036-2, PII S0014579398000362
    • Levy LM, et al. (1998) Inducible expression of the GLT-1 glutamate transporter in a CHO cell line selected for low endogenous glutamate uptake. FEBS Lett 422:339-342. (Pubitemid 28075490)
    • (1998) FEBS Letters , vol.422 , Issue.3 , pp. 339-342
    • Levy, L.M.1    Attwell, D.2    Hoover, F.3    Ash, J.F.4    Bjoras, M.5    Danbolt, N.C.6
  • 4
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • 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
  • 5
    • 0029142729 scopus 로고
    • Ion fluxes associated with excitatory amino acid transport
    • 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
  • 6
    • 33750470835 scopus 로고    scopus 로고
    • Activation of a presynaptic glutamate transporter regulates synaptic transmission through electrical signaling
    • DOI 10.1038/nn1793, PII NN1793
    • Veruki ML, Morkve SH, Hartveit E (2006) Activation of a presynaptic glutamate transporter regulates synaptic transmission through electrical signaling. Nat Neurosci 9:1388-1396. (Pubitemid 44646211)
    • (2006) Nature Neuroscience , vol.9 , Issue.11 , pp. 1388-1396
    • Veruki, M.L.1    Morkve, S.H.2    Hartveit, E.3
  • 7
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O (1966) Simple allosteric model for membrane pumps. Nature 211:969-970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 8
    • 78149499345 scopus 로고    scopus 로고
    • New views of glutamate transporter structure and function: Advances and challenges
    • Jiang J, Amara SG (2011) New views of glutamate transporter structure and function: Advances and challenges. Neuropharmacology 60:172-181.
    • (2011) Neuropharmacology , vol.60 , pp. 172-181
    • Jiang, J.1    Amara, S.G.2
  • 9
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • DOI 10.1038/nature03018
    • Yernool D, Boudker O, Jin Y, Gouaux E (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431:811-818. (Pubitemid 39434071)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 10
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • DOI 10.1038/nature05455, PII NATURE05455
    • 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. (Pubitemid 46160902)
    • (2007) Nature , vol.445 , Issue.7126 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 11
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanism of a bacterial homologue of glutamate transporters
    • 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
  • 12
    • 0037119481 scopus 로고    scopus 로고
    • A hydrophobic domain in glutamate transporters forms an extracellular helix associated with the permeation pathway for substrates
    • Leighton BH, Seal RP, Shimamoto K, Amara SG (2002) A hydrophobic domain in glutamate transporters forms an extracellular helix associated with the permeation pathway for substrates. J Biol Chem 277:29847-29855.
    • (2002) J Biol Chem , vol.277 , pp. 29847-29855
    • Leighton, B.H.1    Seal, R.P.2    Shimamoto, K.3    Amara, S.G.4
  • 13
    • 0037135617 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis reveals a conformationally sensitive reentrant pore-loop in the glutamate transporter GLT-1
    • DOI 10.1074/jbc.M202248200
    • Grunewald M, Menaker D, Kanner BI (2002) Cysteine-scanning mutagenesis reveals a conformationally sensitive reentrant pore-loop in the glutamate transporter GLT-1. J Biol Chem 277:26074-26080. (Pubitemid 34967090)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26074-26080
    • Grunewald, M.1    Menaker, D.2    Kanner, B.I.3
  • 14
    • 57649119782 scopus 로고    scopus 로고
    • Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter
    • 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.
    • (2008) J Biol Chem , vol.283 , pp. 28680-28690
    • Shrivastava, I.H.1    Jiang, J.2    Amara, S.G.3    Bahar, I.4
  • 16
    • 34247484434 scopus 로고    scopus 로고
    • Conformationally sensitive reactivity to permeant sulfhydryl reagents of cysteine residues engineered into helical hairpin 1 of the glutamate transporter GLT-1
    • DOI 10.1124/mol.106.032607
    • Shlaifer I, Kanner BI (2007) Conformationally sensitive reactivity to permeant sulfhydryl reagents of cysteine residues engineered into helical hairpin 1 of the glutamate transporter GLT-1. Mol Pharmacol 71:1341-1348. (Pubitemid 46658687)
    • (2007) Molecular Pharmacology , vol.71 , Issue.5 , pp. 1341-1348
    • Shlaifer, I.1    Kanner, B.I.2
  • 17
    • 73949133608 scopus 로고    scopus 로고
    • Inward-facing conformation of glutamate transporters as revealed by their inverted-topology structural repeats
    • 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
  • 18
    • 33749558576 scopus 로고    scopus 로고
    • Structural rearrangements at the translocation pore of the human glutamate transporter, EAAT1
    • DOI 10.1074/jbc.M604991200
    • Leighton BH, Seal RP, Watts SD, Skyba MO, Amara SG (2006) Structural rearrangements at the translocation pore of the human glutamate transporter, EAAT1. J Biol Chem 281:29788-29796. (Pubitemid 44536988)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , pp. 29788-29796
    • Leighton, B.H.1    Seal, R.P.2    Watts, S.D.3    Skyba, M.O.4    Amara, S.G.5
  • 19
    • 2442693929 scopus 로고    scopus 로고
    • The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway
    • DOI 10.1074/jbc.M304433200
    • 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. (Pubitemid 38656471)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 20742-20751
    • Ryan, R.M.1    Mitrovic, A.D.2    Vandenberg, R.J.3
  • 20
    • 0023034995 scopus 로고
    • The crystallographically determined structures of atypical strained disulfides engineered into subtilisin
    • Katz BA, Kossiakoff A (1986) The crystallographically determined structures of atypical strained disulfides engineered into subtilisin. J Biol Chem 261:15480-15485. (Pubitemid 17208770)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.33 , pp. 15480-15485
    • Katz, B.A.1    Kossiakoff, A.2
  • 21
    • 0023815085 scopus 로고
    • Structure of a bacterial sensory receptor. A site-directed sulfhydryl study
    • Falke JJ, et al. (1988) Structure of a bacterial sensory receptor. A site-directed sulfhydryl study. J Biol Chem 263:14850-14858.
    • (1988) J Biol Chem , vol.263 , pp. 14850-14858
    • Falke, J.J.1
  • 22
    • 0035132230 scopus 로고    scopus 로고
    • Anisotropy of fluctuation dynamics of proteins with an elastic network model
    • Atilgan AR, et al. (2001) Anisotropy of fluctuation dynamics of proteins with an elastic network model. Biophys J 80:505-515.
    • (2001) Biophys J , vol.80 , pp. 505-515
    • Atilgan, A.R.1
  • 23
    • 77949634796 scopus 로고    scopus 로고
    • Normal mode analysis of biomolecular structures: Functional mechanisms of membrane proteins
    • Bahar I, Lezon TR, Bakan A, Shrivastava IH (2010) Normal mode analysis of biomolecular structures: Functional mechanisms of membrane proteins. Chem Rev 110:1463-1497.
    • (2010) Chem Rev , vol.110 , pp. 1463-1497
    • Bahar, I.1    Lezon, T.R.2    Bakan, A.3    Shrivastava, I.H.4
  • 24
    • 33750407288 scopus 로고    scopus 로고
    • Anisotropic network model: Systematic evaluation and a new web interface
    • DOI 10.1093/bioinformatics/btl448
    • Eyal E, Yang LW, Bahar I (2006) Anisotropic network model: Systematic evaluation and a new web interface. Bioinformatics 22:2619-2627. (Pubitemid 44642600)
    • (2006) Bioinformatics , vol.22 , Issue.21 , pp. 2619-2627
    • Eyal, E.1    Yang, L.-W.2    Bahar, I.3
  • 25
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: Bridging between structure and function
    • Bahar I, Lezon TR, Yang LW, Eyal E (2010) Global dynamics of proteins: Bridging between structure and function. Annu Rev Biophys 39:23-42.
    • (2010) Annu Rev Biophys , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Yang, L.W.3    Eyal, E.4
  • 27
    • 24344507684 scopus 로고    scopus 로고
    • Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other
    • DOI 10.1021/bi050987n
    • Grewer C, et al. (2005) Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other. Biochemistry (Mosc) 44:11913-11923. (Pubitemid 41262726)
    • (2005) Biochemistry , vol.44 , Issue.35 , pp. 11913-11923
    • Grewer, C.1    Balani, P.2    Weidenfeller, C.3    Bartusel, T.4    Tao, Z.5    Rauen, T.6
  • 28
    • 33947318986 scopus 로고    scopus 로고
    • The glutamate-activated anion conductance in excitatory amino acid transporters is gated independently by the individual subunits
    • DOI 10.1523/JNEUROSCI.0118-07.2007
    • 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. (Pubitemid 46438962)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2943-2947
    • Koch, H.P.1    Brown, R.L.2    Larsson, H.P.3
  • 29
    • 34548148634 scopus 로고    scopus 로고
    • Rigidity of the Subunit Interfaces of the Trimeric Glutamate Transporter GltT During Translocation
    • DOI 10.1016/j.jmb.2007.06.067, PII S0022283607008741
    • Groeneveld M, Slotboom DJ (2007) Rigidity of the subunit interfaces of the trimeric glutamate transporter GltT during translocation. J Mol Biol 372:565-570. (Pubitemid 47313480)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 565-570
    • Groeneveld, M.1    Slotboom, D.-J.2
  • 30
    • 36549043024 scopus 로고    scopus 로고
    • Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
    • DOI 10.1016/j.sbi.2007.09.011, PII S0959440X07001534, Catalysis and Regulation /Protein
    • Bahar I, Chennubhotla C, Tobi D (2007) Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation. Curr Opin Struct Biol 17:633-640. (Pubitemid 350180409)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.6 , pp. 633-640
    • Bahar, I.1    Chennubhotla, C.2    Tobi, D.3
  • 31
    • 30044434744 scopus 로고    scopus 로고
    • Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state
    • DOI 10.1073/pnas.0507603102
    • Tobi D, Bahar I (2005) Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state. Proc Natl Acad Sci USA 102:18908-18913. (Pubitemid 43049540)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.52 , pp. 18908-18913
    • Tobi, D.1    Bahar, I.2
  • 32
    • 14044263640 scopus 로고    scopus 로고
    • Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters
    • DOI 10.1523/JNEUROSCI.4138-04.2005
    • Koch HP, Larsson HP (2005) Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters. J Neurosci 25:1730-1736. (Pubitemid 40279278)
    • (2005) Journal of Neuroscience , vol.25 , Issue.7 , pp. 1730-1736
    • Koch, H.P.1    Larsson, H.P.2
  • 33
    • 33746064534 scopus 로고    scopus 로고
    • Intersubunit interactions in EAAT4 glutamate transporters
    • DOI 10.1523/JNEUROSCI.4545-05.2006
    • Torres-Salazar D, Fahlke C (2006) Intersubunit interactions in EAAT4 glutamate transporters. J Neurosci 26:7513-7522. (Pubitemid 44315220)
    • (2006) Journal of Neuroscience , vol.26 , Issue.28 , pp. 7513-7522
    • Torres-Salazar, D.1    Fahlke, C.2
  • 34
    • 0025305260 scopus 로고
    • The role of cytosolic and membrane factors in processing of the human beta-2 adrenergic receptor following translocation and glycosylation in a cell-free system
    • Kobilka BK (1990) The role of cytosolic and membrane factors in processing of the human beta-2 adrenergic receptor following translocation and glycosylation in a cell-free system. J Biol Chem 265:7610-7618.
    • (1990) J Biol Chem , vol.265 , pp. 7610-7618
    • Kobilka, B.K.1
  • 35
    • 0031718927 scopus 로고    scopus 로고
    • Transmembrane topology mapping using biotin-containing sulfhydryl reagents
    • DOI 10.1016/S0076-6879(98)96024-4
    • Seal RP, Leighton BH, Amara SG (1998) Transmembrane topology mapping using biotin-containing sulfhydryl reagents. Methods Enzymol 296:318-331. (Pubitemid 28455030)
    • (1998) Methods in Enzymology , vol.296 , pp. 318-331
    • Seal, R.P.1    Leighton, B.H.2    Amara, S.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.