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Volumn 31, Issue 40, 2011, Pages 14095-14106

Chloride ions in the pore of glycine and GABA channels shape the time course and voltage dependence of agonist currents

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID RECEPTOR; CHLORIDE ION; GLYCINE RECEPTOR; THIOCYANATE;

EID: 80053635399     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.1985-11.2011     Document Type: Article
Times cited : (35)

References (59)
  • 2
    • 0020039255 scopus 로고
    • Inhibitory postsynaptic currents at Aplysia cholinergic synapses: Effects of permeant anions and depressant drugs
    • Adams DJ, Gage PW, Hamill OP (1982) Inhibitory postsynaptic currents at Aplysia cholinergic synapses: effects of permeant anions and depressant drugs. Proc R Soc Lond B Biol Sci 214:335-350.
    • (1982) Proc R Soc Lond B Biol Sci , vol.214 , pp. 335-350
    • Adams, D.J.1    Gage, P.W.2    Hamill, O.P.3
  • 3
    • 0018199151 scopus 로고
    • Life time and elementary conductance of the channels mediating the excitatory effects of acetylcholine in Aplysia neurones
    • Ascher P, Marty A, Neild TO (1978) Life time and elementary conductance of the channels mediating the excitatory effects of acetylcholine in Aplysia neurones. J Physiol 278:177-206.
    • (1978) J Physiol , vol.278 , pp. 177-206
    • Ascher, P.1    Marty, A.2    Neild, T.O.3
  • 5
    • 0035999833 scopus 로고    scopus 로고
    • Openings of the rat recombinant a 1 homomeric glycine receptor as a function of the number of agonist molecules bound
    • Beato M, Groot-Kormelink PJ, Colquhoun D, Sivilotti LG (2002) Openings of the rat recombinant a 1 homomeric glycine receptor as a function of the number of agonist molecules bound. J Gen Physiol 119:443-466.
    • (2002) J Gen Physiol , vol.119 , pp. 443-466
    • Beato, M.1    Groot-Kormelink, P.J.2    Colquhoun, D.3    Sivilotti, L.G.4
  • 8
    • 0023162271 scopus 로고
    • Mechanism of anion permeation through channels gated by glycine and y-aminobutyric acid in mouse cultured spinal neurones
    • Bormann J, Hamill OP, Sakmann B (1987) Mechanism of anion permeation through channels gated by glycine and y-aminobutyric acid in mouse cultured spinal neurones. J Physiol 385:243-286.
    • (1987) J Physiol , vol.385 , pp. 243-286
    • Bormann, J.1    Hamill, O.P.2    Sakmann, B.3
  • 9
    • 0346258343 scopus 로고    scopus 로고
    • Stoichiometry of recombinant heteromeric glycine receptors revealed by a pore-lining region point mutation
    • Burzomato V, Groot-Kormelink PJ, Sivilotti LG, Beato M (2003) Stoichiometry of recombinant heteromeric glycine receptors revealed by a pore-lining region point mutation. Receptors Channels 9:353-361.
    • (2003) Receptors Channels , vol.9 , pp. 353-361
    • Burzomato, V.1    Groot-Kormelink, P.J.2    Sivilotti, L.G.3    Beato, M.4
  • 10
    • 0025789972 scopus 로고
    • Effects of pipette geometry on the time course of solution change in patch clamp experiments
    • Cannell MB, Nichols CG (1991) Effects of pipette geometry on the time course of solution change in patch clamp experiments. Biophys J 60:1156-1163.
    • (1991) Biophys J , vol.60 , pp. 1156-1163
    • Cannell, M.B.1    Nichols, C.G.2
  • 12
    • 0029876527 scopus 로고    scopus 로고
    • Transmitter timecourse in the synaptic cleft: Its role in central synaptic function
    • Clements JD (1996) Transmitter timecourse in the synaptic cleft: its role in central synaptic function. Trends Neurosci 19:163-171.
    • (1996) Trends Neurosci , vol.19 , pp. 163-171
    • Clements, J.D.1
  • 14
    • 30744470883 scopus 로고    scopus 로고
    • Probing ion-channel pores one proton at a time
    • Cymes GD, Ni Y, Grosman C (2005) Probing ion-channel pores one proton at a time. Nature 438:975-980.
    • (2005) Nature , vol.438 , pp. 975-980
    • Cymes, G.D.1    Ni, Y.2    Grosman, C.3
  • 15
    • 0002236344 scopus 로고
    • An efficient method for computing synaptic conductances based on a kinetic-model of receptor-binding
    • Destexhe A, Mainen ZF, Sejnowski TJ (1994) An efficient method for computing synaptic conductances based on a kinetic-model of receptor-binding. Neural Comput 6:14-18.
    • (1994) Neural Comput , vol.6 , pp. 14-18
    • Destexhe, A.1    Mainen, Z.F.2    Sejnowski, T.J.3
  • 16
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 17
    • 0028902550 scopus 로고
    • Mechanisms of activation of muscle nicotinic acetylcholine receptors, and the time course of endplate currents
    • Edmonds B, Gibb AJ, Colquhoun D (1995) Mechanisms of activation of muscle nicotinic acetylcholine receptors, and the time course of endplate currents. Annu Rev Physiol 57:469-493.
    • (1995) Annu Rev Physiol , vol.57 , pp. 469-493
    • Edmonds, B.1    Gibb, A.J.2    Colquhoun, D.3
  • 18
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford PJ (1985) A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J Med Chem 28:849-857.
    • (1985) J Med Chem , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 19
    • 0037196236 scopus 로고    scopus 로고
    • Achieving optimal expression for single channel recording: A plasmid ratio approach to the expression of a1 glycine receptors in HEK293 cells
    • Groot-Kormelink PJ, Beato M, Finotti C, Harvey RJ, Sivilotti LG (2002) Achieving optimal expression for single channel recording: a plasmid ratio approach to the expression of a1 glycine receptors in HEK293 cells. J Neurosci Methods 113:207-214.
    • (2002) J Neurosci Methods , vol.113 , pp. 207-214
    • Groot-Kormelink, P.J.1    Beato, M.2    Finotti, C.3    Harvey, R.J.4    Sivilotti, L.G.5
  • 20
    • 61349137676 scopus 로고    scopus 로고
    • An ion selectivity filter in the extracellular domain of Cys-loop receptors reveals determinants for ion conductance
    • Hansen SB, Wang HL, Taylor P, Sine SM (2008) An ion selectivity filter in the extracellular domain of Cys-loop receptors reveals determinants for ion conductance. J Biol Chem 283:36066-36070.
    • (2008) J Biol Chem , vol.283 , pp. 36066-36070
    • Hansen, S.B.1    Wang, H.L.2    Taylor, P.3    Sine, S.M.4
  • 21
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • Hibbs RE, Gouaux E (2011) Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 474:54-60.
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 22
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf RJ, Dutzler R (2008) X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452:375-379.
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 23
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf RJ, Dutzler R (2009) Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457:115-118.
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 25
    • 69049109851 scopus 로고    scopus 로고
    • Intracellular chloride ions regulate the time course of GABA-mediated inhibitory synaptic transmission
    • Houston CM, Bright DP, Sivilotti LG, Beato M, Smart TG (2009) Intracellular chloride ions regulate the time course of GABA-mediated inhibitory synaptic transmission. J Neurosci 29:10416-10423.
    • (2009) J Neurosci , vol.29 , pp. 10416-10423
    • Houston, C.M.1    Bright, D.P.2    Sivilotti, L.G.3    Beato, M.4    Smart, T.G.5
  • 26
    • 34447131659 scopus 로고    scopus 로고
    • Barriers to ion translocation in cationic and anionic receptors from the Cys-loop family
    • Ivanov I, Cheng X, Sine SM, McCammon JA (2007) Barriers to ion translocation in cationic and anionic receptors from the Cys-loop family. J Am Chem Soc 129:8217-8224.
    • (2007) J Am Chem Soc , vol.129 , pp. 8217-8224
    • Ivanov, I.1    Cheng, X.2    Sine, S.M.3    McCammon, J.A.4
  • 27
    • 38749094806 scopus 로고    scopus 로고
    • Modular design of Cys-loop ligand-gated ion channels: Functional 5-HT3 and GABA rho1 receptors lacking the large cytoplasmic M3M4 loop
    • Jansen M, Bali M, Akabas MH (2008) Modular design of Cys-loop ligand-gated ion channels: functional 5-HT3 and GABA rho1 receptors lacking the large cytoplasmic M3M4 loop. J Gen Physiol 131:137-146.
    • (2008) J Gen Physiol , vol.131 , pp. 137-146
    • Jansen, M.1    Bali, M.2    Akabas, M.H.3
  • 29
    • 0033916254 scopus 로고    scopus 로고
    • M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective
    • Keramidas A, Moorhouse AJ, French CR, Schofield PR, Barry PH (2000) M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective. Biophys J 79:247-259.
    • (2000) Biophys J , vol.79 , pp. 247-259
    • Keramidas, A.1    Moorhouse, A.J.2    French, C.R.3    Schofield, P.R.4    Barry, P.H.5
  • 30
    • 0035999831 scopus 로고    scopus 로고
    • Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity
    • Keramidas A, Moorhouse AJ, Pierce KD, Schofield PR, Barry PH (2002) Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity. J Gen Physiol 119:393-410.
    • (2002) J Gen Physiol , vol.119 , pp. 393-410
    • Keramidas, A.1    Moorhouse, A.J.2    Pierce, K.D.3    Schofield, P.R.4    Barry, P.H.5
  • 31
    • 0027764470 scopus 로고
    • Importance of Arg-219 for correct biogenesis of a1 homooligomeric glycine receptors
    • Langosch D, Herbold A, Schmieden V, Borman J, Kirsch J (1993) Importance of Arg-219 for correct biogenesis of a1 homooligomeric glycine receptors. FEBS Lett 336:540-544.
    • (1993) FEBS Lett , vol.336 , pp. 540-544
    • Langosch, D.1    Herbold, A.2    Schmieden, V.3    Borman, J.4    Kirsch, J.5
  • 32
    • 0028016521 scopus 로고
    • Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia
    • Langosch D, Laube B, Rundstrom N, Schmieden V, Bormann J, Betz H (1994) Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia. EMBO J 13:4223-4228.
    • (1994) EMBO J , vol.13 , pp. 4223-4228
    • Langosch, D.1    Laube, B.2    Rundstrom, N.3    Schmieden, V.4    Bormann, J.5    Betz, H.6
  • 33
    • 0000243829 scopus 로고
    • PRO-CHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PRO-CHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0032693373 scopus 로고    scopus 로고
    • Voltage dependence of the glycine receptor-channel kinetics in the zebrafish hindbrain
    • Legendre P (1999) Voltage dependence of the glycine receptor-channel kinetics in the zebrafish hindbrain. J Neurophysiol 82:2120-2129.
    • (1999) J Neurophysiol , vol.82 , pp. 2120-2129
    • Legendre, P.1
  • 35
    • 0032520102 scopus 로고    scopus 로고
    • Properties of human glycine receptors containing the hyperekplexia mutation a1(K276E), expressed in Xenopus oocytes
    • Lewis TM, Sivilotti LG, Colquhoun D, Gardiner RM, Schoepfer R, Rees M (1998) Properties of human glycine receptors containing the hyperekplexia mutation a1(K276E), expressed in Xenopus oocytes. J Physiol 507:25-40.
    • (1998) J Physiol , vol.507 , pp. 25-40
    • Lewis, T.M.1    Sivilotti, L.G.2    Colquhoun, D.3    Gardiner, R.M.4    Schoepfer, R.5    Rees, M.6
  • 36
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Mod (Berl) 7:306-317.
    • (2001) J Mol Mod (Berl) , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 37
    • 0000830676 scopus 로고    scopus 로고
    • Diffusion coefficients in aqueous solutions of potassium chloride at high and low concentrations
    • Lobo VMM, Ribeiro ACF, Verissimo LMP (1998) Diffusion coefficients in aqueous solutions of potassium chloride at high and low concentrations. J Mol Liq 78:139-149.
    • (1998) J Mol Liq , vol.78 , pp. 139-149
    • Lobo, V.M.M.1    Ribeiro, A.C.F.2    Verissimo, L.M.P.3
  • 38
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • Lynch JW, Rajendra S, Pierce KD, Handford CA, Barry PH, Schofield PR (1997) Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel. EMBO J 16:110-120.
    • (1997) EMBO J , vol.16 , pp. 110-120
    • Lynch, J.W.1    Rajendra, S.2    Pierce, K.D.3    Handford, C.A.4    Barry, P.H.5    Schofield, P.R.6
  • 39
    • 0015339664 scopus 로고
    • The effect of voltage on the time course of end-plate currents
    • Magleby KL, Stevens CF (1972) The effect of voltage on the time course of end-plate currents. J Physiol 223:151-171.
    • (1972) J Physiol , vol.223 , pp. 151-171
    • Magleby, K.L.1    Stevens, C.F.2
  • 40
    • 0018651927 scopus 로고
    • Interaction of permeant ions with channels activated by acetylcholine in Aplysia neurones
    • Marchais D, Marty A (1979) Interaction of permeant ions with channels activated by acetylcholine in Aplysia neurones. J Physiol 297:9-45.
    • (1979) J Physiol , vol.297 , pp. 9-45
    • Marchais, D.1    Marty, A.2
  • 41
    • 79953874257 scopus 로고    scopus 로고
    • A channels, different subunits contribute asymmetrically to channel conductance via residues in the extracellular domain
    • Moroni M, Meyer JO, Lahmann C, Sivilotti LG (2011) In glycine and GABAA channels, different subunits contribute asymmetrically to channel conductance via residues in the extracellular domain. J Biol Chem 286:13414-13422.
    • (2011) J Biol Chem , vol.286 , pp. 13414-13422
    • Moroni, M.1    Meyer, J.O.2    Lahmann, C.3    Sivilotti, L.G.4
  • 42
    • 0023701515 scopus 로고
    • Calculation of time constants for intracellular diffusion in whole cell patch clamp configuration
    • Oliva C, Cohen IS, Mathias RT (1988) Calculation of time constants for intracellular diffusion in whole cell patch clamp configuration. Biophys J 54:791-799.
    • (1988) Biophys J , vol.54 , pp. 791-799
    • Oliva, C.1    Cohen, I.S.2    Mathias, R.T.3
  • 43
    • 17844374081 scopus 로고    scopus 로고
    • A receptor examined using Brownian dynamics
    • O'Mara M, Cromer B, Parker M, Chung SH (2005) Homology model of the GABAA receptor examined using Brownian dynamics. Biophys J 88:3286-3299.
    • (2005) Biophys J , vol.88 , pp. 3286-3299
    • O'Mara, M.1    Cromer, B.2    Parker, M.3    Chung, S.H.4
  • 44
    • 0018333420 scopus 로고
    • An analysis of the inhibitory postsynaptic current in the voltage-clamped crayfish muscle
    • Onodera K, Takeuchi A (1979) An analysis of the inhibitory postsynaptic current in the voltage-clamped crayfish muscle. J Physiol 286:265-282.
    • (1979) J Physiol , vol.286 , pp. 265-282
    • Onodera, K.1    Takeuchi, A.2
  • 46
    • 77949521702 scopus 로고    scopus 로고
    • Novel structural determinants of single channel conductance and ion selectivity in 5-hydroxytryptamine type 3 and nicotinic acetylcholine receptors
    • Peters JA, Cooper MA, Carland JE, Livesey MR, Hales TG, Lambert JJ (2010) Novel structural determinants of single channel conductance and ion selectivity in 5-hydroxytryptamine type 3 and nicotinic acetylcholine receptors. J Physiol 588:587-596.
    • (2010) J Physiol , vol.588 , pp. 587-596
    • Peters, J.A.1    Cooper, M.A.2    Carland, J.E.3    Livesey, M.R.4    Hales, T.G.5    Lambert, J.J.6
  • 47
    • 58149264819 scopus 로고    scopus 로고
    • High intracellular chloride slows the decay of glycinergic currents
    • Pitt SJ, Sivilotti LG, Beato M (2008) High intracellular chloride slows the decay of glycinergic currents. J Neurosci 28:11454-11467.
    • (2008) J Neurosci , vol.28 , pp. 11454-11467
    • Pitt, S.J.1    Sivilotti, L.G.2    Beato, M.3
  • 48
    • 77956193129 scopus 로고    scopus 로고
    • Probing pore constriction in a ligand-gated ion channel by trapping a metal ion in the pore upon agonist dissociation
    • Pittel I, Witt-Kehati D, Degani-Katzav N, Paas Y (2010) Probing pore constriction in a ligand-gated ion channel by trapping a metal ion in the pore upon agonist dissociation. J Biol Chem 285:26519-26531.
    • (2010) J Biol Chem , vol.285 , pp. 26519-26531
    • Pittel, I.1    Witt-Kehati, D.2    Degani-Katzav, N.3    Paas, Y.4
  • 50
    • 0036977495 scopus 로고    scopus 로고
    • Functional characterization of compound heterozygosity for GlyRa1 mutations in the startle disease hyperekplexia
    • Rea R, Tijssen MA, Herd C, Frants RR, Kullmann DM (2002) Functional characterization of compound heterozygosity for GlyRa1 mutations in the startle disease hyperekplexia. Eur J Neurosci 16:186-196.
    • (2002) Eur J Neurosci , vol.16 , pp. 186-196
    • Rea, R.1    Tijssen, M.A.2    Herd, C.3    Frants, R.R.4    Kullmann, D.M.5
  • 51
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 52
    • 0027330927 scopus 로고
    • Mutations in the a1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia
    • Shiang R, Ryan SG, Zhu YZ, Hahn AF, O'Connell P, Wasmuth JJ (1993) Mutations in the a1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia. Nat Genet 5:351-358.
    • (1993) Nat Genet , vol.5 , pp. 351-358
    • Shiang, R.1    Ryan, S.G.2    Zhu, Y.Z.3    Hahn, A.F.4    O'Connell, P.5    Wasmuth, J.J.6
  • 53
    • 76249132103 scopus 로고    scopus 로고
    • Ion conduction in ligand-gated ion channels: Brownian dynamics studies of four recent crystal structures
    • Song C, Corry B (2010) Ion conduction in ligand-gated ion channels: Brownian dynamics studies of four recent crystal structures. Biophys J 98:404 -411.
    • (2010) Biophys J , vol.98 , pp. 404-411
    • Song, C.1    Corry, B.2
  • 54
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4Å resolution
    • Unwin N (2005) Refined structure of the nicotinic acetylcholine receptor at 4Å resolution. J Mol Biol 346:967-989.
    • (2005) J Mol Biol , vol.346 , pp. 967-989
    • Unwin, N.1
  • 56
    • 0017707361 scopus 로고
    • Permeant cations alter endplate channel characteristics
    • Van Helden D, Hamill OP, Gage PW (1977) Permeant cations alter endplate channel characteristics. Nature 269:711-713.
    • (1977) Nature , vol.269 , pp. 711-713
    • van Helden, D.1    Hamill, O.P.2    Gage, P.W.3
  • 57
    • 0001823013 scopus 로고    scopus 로고
    • Single-channel activations and concentration jumps: Comparison of recombinant NR1a/NR2A and NR1a/NR2D NMDA receptors
    • Wyllie DJ, Behe P, Colquhoun D (1998) Single-channel activations and concentration jumps: comparison of recombinant NR1a/NR2A and NR1a/NR2D NMDA receptors. J Physiol 510:1-18.
    • (1998) J Physiol , vol.510 , pp. 1-18
    • Wyllie, D.J.1    Behe, P.2    Colquhoun, D.3
  • 58
    • 0027501362 scopus 로고
    • Amino acids lining the channel of the y-aminobutyric acid type A receptor identified by cysteine substitution
    • Xu M, Akabas MH (1993) Amino acids lining the channel of the y-aminobutyric acid type A receptor identified by cysteine substitution. J Biol Chem 268:21505-21508.
    • (1993) J Biol Chem , vol.268 , pp. 21505-21508
    • Xu, M.1    Akabas, M.H.2
  • 59
    • 0029865892 scopus 로고    scopus 로고
    • A receptor alpha1 subunit
    • Xu M, Akabas MH (1996) Identification of channel-lining residues in the M2 membrane-spanning segment of the GABAA receptor alpha1 subunit. J Gen Physiol 107:195-205.
    • (1996) J Gen Physiol , vol.107 , pp. 195-205
    • Xu, M.1    Akabas, M.H.2


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