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Volumn 79, Issue 1, 2000, Pages 247-259

M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective

Author keywords

[No Author keywords available]

Indexed keywords

ANION CHANNEL; CALCIUM ION; CATION CHANNEL; CHOLINERGIC RECEPTOR; GLYCINE RECEPTOR; MUTANT PROTEIN; RECEPTOR PROTEIN; SODIUM CHLORIDE;

EID: 0033916254     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76287-4     Document Type: Article
Times cited : (104)

References (43)
  • 1
    • 0018894860 scopus 로고
    • The permeability of endplate channels to monovalent and divalent metal cations
    • Adams, D. J., T. M. Dwyer, and B. Hille. 1980. The permeability of endplate channels to monovalent and divalent metal cations. J. Gen. Physiol. 75:493-510.
    • (1980) J. Gen. Physiol. , vol.75 , pp. 493-510
    • Adams, D.J.1    Dwyer, T.M.2    Hille, B.3
  • 2
    • 0028351818 scopus 로고
    • JPCalc, a software package for calculating liquid junction potential corrections in patch-clamp, intracellular, epithelial and bilayer measurements and for correcting junction potential measurements
    • Barry, P. H. 1994. JPCalc, a software package for calculating liquid junction potential corrections in patch-clamp, intracellular, epithelial and bilayer measurements and for correcting junction potential measurements. J. Neurosci. Meth. 51:107-116.
    • (1994) J. Neurosci. Meth. , vol.51 , pp. 107-116
    • Barry, P.H.1
  • 3
    • 0001802726 scopus 로고
    • Ion selectivity of channels at the end-plate
    • W. D. Stein, editor. Academic Press, London
    • Barry, P. H., and P. W. Gage. 1984. Ion selectivity of channels at the end-plate. In Current Topics in Membranes and Transport. W. D. Stein, editor. Academic Press, London. 21:1-51.
    • (1984) Current Topics in Membranes and Transport , vol.21 , pp. 1-51
    • Barry, P.H.1    Gage, P.W.2
  • 4
    • 0025774354 scopus 로고
    • Liquid junction potentials and small cell effects in patch-clamp analysis
    • Barry, P. H., and J. W. Lynch. 1991. Liquid junction potentials and small cell effects in patch-clamp analysis. J. Membr. Biol. 121:101-107.
    • (1991) J. Membr. Biol. , vol.121 , pp. 101-107
    • Barry, P.H.1    Lynch, J.W.2
  • 5
    • 0027214596 scopus 로고
    • Mutations at two distinct sites within the channel domain M2 alter calcium permeability of neuronal α7 nicotinic receptor
    • Bertrand, D., J. L. Galzi, A. Devillers-Thiéry, S. Bertrand, and J. P. Changeux. 1993. Mutations at two distinct sites within the channel domain M2 alter calcium permeability of neuronal α7 nicotinic receptor. Proc. Natl. Acad. Sci. USA. 90:6971-6975.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6971-6975
    • Bertrand, D.1    Galzi, J.L.2    Devillers-Thiéry, A.3    Bertrand, S.4    Changeux, J.P.5
  • 6
    • 0023162271 scopus 로고
    • Mechanism of anion permeation through channels gated by glycine and GABA in mouse cultured spinal neurons
    • Bormann, J., O. P. Hamill, and B. Sakmann. 1987. Mechanism of anion permeation through channels gated by glycine and GABA in mouse cultured spinal neurons. J. Physiol. (Lond.). 385:243-286.
    • (1987) J. Physiol. (Lond.) , vol.385 , pp. 243-286
    • Bormann, J.1    Hamill, O.P.2    Sakmann, B.3
  • 7
    • 0027224010 scopus 로고
    • Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers
    • Bormann, J., N. Rundstrom, H. Betz, and D. Langosch. 1993. Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers. EMBO J. 12:3729-3737.
    • (1993) EMBO J. , vol.12 , pp. 3729-3737
    • Bormann, J.1    Rundstrom, N.2    Betz, H.3    Langosch, D.4
  • 8
    • 0023392945 scopus 로고
    • High efficiency expression of mammalian cells by plasmid DNA
    • Chen, C., and H. Okayama. 1987. High efficiency expression of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2751.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2751
    • Chen, C.1    Okayama, H.2
  • 9
    • 0033119869 scopus 로고    scopus 로고
    • Mutational analysis of the charge selectivity filter of the α7 nicotinic acetylcholine receptor
    • Corringer, P. J., S. Bertrand, J. L. Galzi, A. Devillers-Thiéry, J. P. Changeux, and D. Bertrand. 1999. Mutational analysis of the charge selectivity filter of the α7 nicotinic acetylcholine receptor. Neuron. 22: 831-843.
    • (1999) Neuron , vol.22 , pp. 831-843
    • Corringer, P.J.1    Bertrand, S.2    Galzi, J.L.3    Devillers-Thiéry, A.4    Changeux, J.P.5    Bertrand, D.6
  • 10
    • 0022626737 scopus 로고
    • Ion-channel entrances influence permeation
    • Dani, J. A. 1986. Ion-channel entrances influence permeation. Biophys. J. 49:607-618.
    • (1986) Biophys. J. , vol.49 , pp. 607-618
    • Dani, J.A.1
  • 11
    • 0021070747 scopus 로고
    • Ionic selectivity revisited: The role of kinetic and equilibrium processes in ion permeation through channels
    • Eisenman, G., and R. Horn. 1983. Ionic selectivity revisited: the role of kinetic and equilibrium processes in ion permeation through channels. J. Membr. Biol. 76:197-225.
    • (1983) J. Membr. Biol. , vol.76 , pp. 197-225
    • Eisenman, G.1    Horn, R.2
  • 12
    • 0027326059 scopus 로고
    • Anion permeation in GABA- and glycine-gated channels of mammalian hippocampal neurons
    • Fatima-Shad, K., and P. H. Barry. 1993. Anion permeation in GABA- and glycine-gated channels of mammalian hippocampal neurons. Proc. R. Soc. Lond. B. 253:69-75.
    • (1993) Proc. R. Soc. Lond. B , vol.253 , pp. 69-75
    • Fatima-Shad, K.1    Barry, P.H.2
  • 13
    • 0026656037 scopus 로고
    • Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
    • Galzi, J. L., A. Devillers-Thiéry, N. Hussey, S. Bertrand, J. P. Changeux, and D. Bertrand. 1992. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature. 359:500-505.
    • (1992) Nature , vol.359 , pp. 500-505
    • Galzi, J.L.1    Devillers-Thiéry, A.2    Hussey, N.3    Bertrand, S.4    Changeux, J.P.5    Bertrand, D.6
  • 14
    • 0010648804 scopus 로고
    • Analysis of whole cell currents to estimate the kinetics and amplitude of unitary events: Relaxation and 'noise' analysis
    • D. Ogden, editor. The Company of Biologists Limited, Cambridge
    • Gray, P. T. A. 1994. Analysis of whole cell currents to estimate the kinetics and amplitude of unitary events: relaxation and 'noise' analysis. In Microelectrode Techniques, 2nd Ed. D. Ogden, editor. The Company of Biologists Limited, Cambridge. 189-207.
    • (1994) Microelectrode Techniques, 2nd Ed. , pp. 189-207
    • Gray, P.T.A.1
  • 16
    • 0025745108 scopus 로고
    • A ring of uncharged polar amino acids as a component of channel constriction in the nicotinic acetylcholine receptor
    • Imoto, K., T. Konno, J. Nakai, F. Wang, M. Mishina, and S. Numa. 1991. A ring of uncharged polar amino acids as a component of channel constriction in the nicotinic acetylcholine receptor. FEBS Lett. 289: 193-200.
    • (1991) FEBS Lett. , vol.289 , pp. 193-200
    • Imoto, K.1    Konno, T.2    Nakai, J.3    Wang, F.4    Mishina, M.5    Numa, S.6
  • 17
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin, A., and M. H. Akabas. 1995. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron. 15:1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 19
    • 0029044590 scopus 로고
    • The inhibitory glycine receptor: Architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex
    • Kuhse, J., H. Betz, and J. Kirsch. 1995. The inhibitory glycine receptor: architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex. Curr. Opin. Neurobiol. 5:318-323.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 318-323
    • Kuhse, J.1    Betz, H.2    Kirsch, J.3
  • 20
    • 0027764470 scopus 로고
    • Importance of Arg-219 for correct biogenesis of α1 homooligomeric glycine receptors
    • Langosch, D., A. Herbold, V. Schmieden, J. Bormann, and J. Kirsch. 1993. Importance of Arg-219 for correct biogenesis of α1 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    Bormann, J.4    Kirsch, J.5
  • 21
    • 0028016521 scopus 로고
    • Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia
    • Langosch, D., B. Laube, N. Rundstrom, V. Schmieden, J. Bormann, and H. Betz. 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
  • 22
    • 0001202076 scopus 로고
    • Conserved quaternary structure of ligand-gated ion channels: The post synaptic glycine receptor is a pentamer
    • Langosch, D., L. Thomas, and H. Betz. 1988. Conserved quaternary structure of ligand-gated ion channels: the post synaptic glycine receptor is a pentamer. Proc. Natl. Acad. Sci. USA. 85:7394-7398.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7394-7398
    • Langosch, D.1    Thomas, L.2    Betz, H.3
  • 23
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • Lynch, J. W., S. Rajendra, K. D. Pierce, C. A. Handford, P. H. Barry, and P. R. Schofield. 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
  • 24
    • 0024623211 scopus 로고
    • Genetic manipulation of ion channels: A new approach to structure and mechanism
    • Miller, C. 1989. Genetic manipulation of ion channels: a new approach to structure and mechanism. Neuron. 2:1195-1205.
    • (1989) Neuron , vol.2 , pp. 1195-1205
    • Miller, C.1
  • 25
    • 0033013979 scopus 로고    scopus 로고
    • The startle disease mutation Q266H, in the second transmembrane domain of the human glycine receptor, impairs gating
    • Moorhouse, A. J., P. Jacques, P. H. Barry, and P. R. Schofield. 1999. The startle disease mutation Q266H, in the second transmembrane domain of the human glycine receptor, impairs gating. Mol. Pharmacol. 55: 386-395.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 386-395
    • Moorhouse, A.J.1    Jacques, P.2    Barry, P.H.3    Schofield, P.R.4
  • 26
    • 0031781630 scopus 로고    scopus 로고
    • State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor
    • Pascual, J. M., and A. Karlin. 1998. State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor. J. Gen. Physiol. 111:171-739.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 171-739
    • Pascual, J.M.1    Karlin, A.2
  • 27
    • 0023186453 scopus 로고
    • Ion permeation through single channels activated by acetylcholine in denervated toad sartorius muscle fibers: Effects of alkali cations
    • Quartararo, N., P. H. Barry, and P. W. Gage. 1987. Ion permeation through single channels activated by acetylcholine in denervated toad sartorius muscle fibers: effects of alkali cations. J. Membr. Biol. 97:137-159.
    • (1987) J. Membr. Biol. , vol.97 , pp. 137-159
    • Quartararo, N.1    Barry, P.H.2    Gage, P.W.3
  • 29
    • 0028361803 scopus 로고
    • Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor
    • Rajendra, S., J. W. Lynch, K. D. Pierce, C. R. French, P. H. Barry, and P. R. Schofield. 1994. Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor. J. Biol. Chem. 269:18739-18742.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18739-18742
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 30
    • 0028831226 scopus 로고
    • Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists to competitive antagonists
    • Rajendra, S., J. W. Lynch, K. D. Pierce, C. R. French, P. H. Barry, and P. R. Schofield. 1995. Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists to competitive antagonists. Neuron. 14:169-175.
    • (1995) Neuron , vol.14 , pp. 169-175
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 32
    • 0029278634 scopus 로고
    • Twist to open
    • Sansom, M. S. P. 1995. Twist to open. Curr. Biol. 5:373-375.
    • (1995) Curr. Biol. , vol.5 , pp. 373-375
    • Sansom, M.S.P.1
  • 33
    • 0033080914 scopus 로고    scopus 로고
    • Novel GLRA1 missense mutation (P250T) in dominant hyperekplexia defines an intracellular determinant of glycine receptor channel gating
    • Saul, B., T. Kuner. D. Sobetzko, W. Brune, F. Hanefeld, H. M. Meinck, and C. M. Becker. 1999. Novel GLRA1 missense mutation (P250T) in dominant hyperekplexia defines an intracellular determinant of glycine receptor channel gating. J. Neurosci. 19:869-877.
    • (1999) J. Neurosci. , vol.19 , pp. 869-877
    • Saul, B.1    Kuner, T.2    Sobetzko, D.3    Brune, W.4    Hanefeld, F.5    Meinck, H.M.6    Becker, C.M.7
  • 35
    • 0028921479 scopus 로고
    • The acetylcholine receptor channel imaged in the open state
    • Unwin, N. 1995. The acetylcholine receptor channel imaged in the open state. Nature. 373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 36
    • 0026700629 scopus 로고
    • Asymmetry of the rat acetylcholine receptor subunits in the narrow region of the pore
    • Villarroel, A., S. Herlitze, V. Witzemann, M. Koenen, and B. Sakmann. 1992. Asymmetry of the rat acetylcholine receptor subunits in the narrow region of the pore. Proc. R. Soc. Lond. B. 249:317-324.
    • (1992) Proc. R. Soc. Lond. B , vol.249 , pp. 317-324
    • Villarroel, A.1    Herlitze, S.2    Witzemann, V.3    Koenen, M.4    Sakmann, B.5
  • 37
    • 0026639439 scopus 로고
    • Threonine in the selectivity filter of the acetylcholine receptor channel
    • Villarroel, A., and B. Sakmann. 1992. Threonine in the selectivity filter of the acetylcholine receptor channel. Biophys. J. 62:196-208.
    • (1992) Biophys. J. , vol.62 , pp. 196-208
    • Villarroel, A.1    Sakmann, B.2
  • 38
    • 0026468667 scopus 로고
    • Pore size and negative charge as structural determinants of permeability in the Torpedo nicotinic acetylcholine receptor channel
    • Wang, F., and K. Imoto. 1992. Pore size and negative charge as structural determinants of permeability in the Torpedo nicotinic acetylcholine receptor channel. Proc. R. Soc. Lond. B. 250:11-17.
    • (1992) Proc. R. Soc. Lond. B , vol.250 , pp. 11-17
    • Wang, F.1    Imoto, K.2
  • 39
    • 0032812829 scopus 로고    scopus 로고
    • Cation permeability and cation-anion interactions in a mutant GABA-gated chloride channel from Drosophila
    • Wang, C. T., H. G. Zhang, T. A. Rocheleau, R. H. ffrench-Constant, and M. B. Jackson. 1999. Cation permeability and cation-anion interactions in a mutant GABA-gated chloride channel from Drosophila. Biophys. J. 77:691-700.
    • (1999) Biophys. J. , vol.77 , pp. 691-700
    • Wang, C.T.1    Zhang, H.G.2    Rocheleau, T.A.3    Ffrench-Constant, R.H.4    Jackson, M.B.5
  • 40
    • 0032102496 scopus 로고    scopus 로고
    • The location of the gate in the acetylcholine receptor channel
    • Wilson, G. G., and A. Karlin. 1998. The location of the gate in the acetylcholine receptor channel. Neuron. 20:1269-1281.
    • (1998) Neuron , vol.20 , pp. 1269-1281
    • Wilson, G.G.1    Karlin, A.2
  • 41
    • 0033813781 scopus 로고    scopus 로고
    • The intrinsic electrostatic potential and the intermediate ring of charge in the acetylcholine receptor channel
    • Wilson, G. G., P. M. Pascual, N. Brooijmans, D. Murray, and A. Karlin. 2000. The intrinsic electrostatic potential and the intermediate ring of charge in the acetylcholine receptor channel. J. Gen. Physiol. 115: 93-106.
    • (2000) J. Gen. Physiol. , vol.115 , pp. 93-106
    • Wilson, G.G.1    Pascual, P.M.2    Brooijmans, N.3    Murray, D.4    Karlin, A.5
  • 43
    • 0028970548 scopus 로고
    • A receptor channel-lining residues probed in cysteine mutants
    • A receptor channel-lining residues probed in cysteine mutants. Biophys. J. 69:1858-1867.
    • (1995) Biophys. J. , vol.69 , pp. 1858-1867
    • Xu, M.1    Covey, D.F.2    Akabas, M.H.3


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