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Volumn 122, Issue 2, 2003, Pages 133-145

Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels

Author keywords

ClC 0; Electrostatic effect; Pore conductance; Surface charge

Indexed keywords

CHLORIDE; CHLORIDE CHANNEL; GLUTAMIC ACID; LYSINE; METHANETHIOSULFONATE; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0042377364     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.200308844     Document Type: Article
Times cited : (63)

References (42)
  • 1
    • 0024331485 scopus 로고
    • Kinetics of ion movement mediated by carriers and channels
    • Andersen, O.S. 1989. Kinetics of ion movement mediated by carriers and channels. Methods Enzymol. 171:62-112.
    • (1989) Methods Enzymol. , vol.171 , pp. 62-112
    • Andersen, O.S.1
  • 2
    • 0026332208 scopus 로고
    • Completely functional double-barreled chloride channel expressed from a single Torpedo cDNA
    • Bauer, C.K., K. Steinmeyer, J.R. Schwarz, and T.J. Jentsch. 1991. Completely functional double-barreled chloride channel expressed from a single Torpedo cDNA. Proc. Natl. Acad. Sci. USA, 88:11052-11056.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11052-11056
    • Bauer, C.K.1    Steinmeyer, K.2    Schwarz, J.R.3    Jentsch, T.J.4
  • 3
    • 0021309504 scopus 로고
    • + channel of sarcoplasmic reticulum
    • + channel of sarcoplasmic reticulum. Biophys. J. 45:279-287.
    • (1984) Biophys. J. , vol.45 , pp. 279-287
    • Bell, J.1    Miller, C.2
  • 4
  • 5
    • 0032407783 scopus 로고    scopus 로고
    • Extacellular zinc ion inhibits ClC-0 chloride channels by facilitating slow gating
    • Chen, T.-Y. 1998. Extacellular zinc ion inhibits ClC-0 chloride channels by facilitating slow gating. J. Gen. Physiol. 112:715-726.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 715-726
    • Chen, T.-Y.1
  • 8
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler, R., E.B. Campbell, M. Cadene, B.T. Chait, and R. MacKinnon. 2002. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415:287-294.
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 9
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., E.B. Campbell, and R. MacKinnon. 2003. Gating the selectivity filter in ClC chloride channels. Science. 300:108-112.
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 10
    • 0031468569 scopus 로고    scopus 로고
    • Pore-forming segments in voltage-gated chloride channels
    • Fahlke, C., H.T. Yu, C.L. Beck, T.H. Rhodes, and A.L. George, Jr. 1997. Pore-forming segments in voltage-gated chloride channels. Nature. 390:529-532.
    • (1997) Nature , vol.390 , pp. 529-532
    • Fahlke, C.1    Yu, H.T.2    Beck, C.L.3    Rhodes, T.H.4    George A.L., Jr.5
  • 11
    • 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. Hussy, 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    Hussy, N.3    Bertrand, S.4    Changeux, J.-P.5    Bertrand, D.6
  • 12
    • 0026026676 scopus 로고
    • Surface charges and ion channel functions
    • Green, W.N., and O.S. Andersen. 1991. Surface charges and ion channel functions. Annu. Rev. Physiol. 53:341-359.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 341-359
    • Green, W.N.1    Andersen, O.S.2
  • 13
    • 0020521341 scopus 로고
    • Single chloride channels from Torpedo electroplax: Activation by protons
    • Hanke, W., and C. Miller. 1983. Single chloride channels from Torpedo electroplax: activation by protons. J. Gen. Physiol. 82:25-45.
    • (1983) J. Gen. Physiol. , vol.82 , pp. 25-45
    • Hanke, W.1    Miller, C.2
  • 14
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O.P., A. Marly, E. Neher, B. Sakmann, and F.J. Sigworth. 1981. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflugers Arch. 391:85-100.
    • (1981) Pflugers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marly, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 15
    • 0041898981 scopus 로고    scopus 로고
    • Elementary properties of ions in solution
    • B. Hille, editor. Sinauer Associates, Inc., Sunderland, MA
    • Hille, B. 2001. Elementary properties of ions in solution. In Ion Channel of Excitable Membrane. 3rd ed. B. Hille, editor. Sinauer Associates, Inc., Sunderland, MA. 309-345.
    • (2001) Ion Channel of Excitable Membrane. 3rd Ed. , pp. 309-345
    • Hille, B.1
  • 18
    • 0037126294 scopus 로고    scopus 로고
    • A biological role for prokaryotic ClC chloride channels
    • Iyer, R., T.M. Iverson, A. Accardi, and C. Miller. 2002. A biological role for prokaryotic ClC chloride channels. Nature. 419:715-718.
    • (2002) Nature , vol.419 , pp. 715-718
    • Iyer, R.1    Iverson, T.M.2    Accardi, A.3    Miller, C.4
  • 20
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • Jentsch, T.J., V. Stein, F. Weinreich, and A. Zdebik. 2002. Molecular structure and physiological function of chloride channels. Physiol. Rev. 82:503-568.
    • (2002) Physiol. Rev. , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.4
  • 21
    • 0025200567 scopus 로고
    • Primary structure of Torpedo marmorota chloride channel isolated by expression cloning in Xenopus oocytes
    • Jentsch, T.J., K. Steinmeyer, and G. Schwarz. 1990. Primary structure of Torpedo marmorota chloride channel isolated by expression cloning in Xenopus oocytes. Nature. 348:510-514.
    • (1990) Nature , vol.348 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 22
    • 0033916254 scopus 로고    scopus 로고
    • M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective
    • Keramidas, A., A.J. Moorhouse, C.R., French, P.R. Schofield, and P.H. Barry. 2000. M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective. Biophys. J. 78:247-259.
    • (2000) Biophys. J. , vol.78 , pp. 247-259
    • Keramidas, A.1    Moorhouse, A.J.2    French, C.R.3    Schofield, P.R.4    Barry, P.H.5
  • 23
    • 0028118783 scopus 로고
    • Conductance mutations of the nicotinic acetylcholine receptor do not act by a simple electrostatic mechanism
    • Kienker, P., G. Tomaselli, M. Jurman, and G. Yellen. 1994. Conductance mutations of the nicotinic acetylcholine receptor do not act by a simple electrostatic mechanism. Biophys. J. 66:25-334.
    • (1994) Biophys. J. , vol.66 , pp. 25-334
    • Kienker, P.1    Tomaselli, G.2    Jurman, M.3    Yellen, G.4
  • 24
    • 0033781187 scopus 로고    scopus 로고
    • Cysteine modification of a putative pore residue in ClC-0: Implication for the pore stoichiometry of ClC chloride channels
    • Lin, C.-W., and T.-Y. Chen. 2000. Cysteine modification of a putative pore residue in ClC-0: implication for the pore stoichiometry of ClC chloride channels. J. Gen. Physiol. 116:535-546.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 535-546
    • Lin, C.-W.1    Chen, T.-Y.2
  • 25
    • 0042377363 scopus 로고    scopus 로고
    • Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents
    • Lin, C.-W., and T.-Y. Chen. 2003. Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents. J. Gen. Physiol. 122:225-237.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 225-237
    • Lin, C.-W.1    Chen, T.-Y.2
  • 26
    • 0033000370 scopus 로고    scopus 로고
    • Elimination of the slow gating of ClC-0 chloride channel by a point mutation
    • Lin, Y.-W., C.-W. Lin, and T.-Y Chen. 1999. Elimination of the slow gating of ClC-0 chloride channel by a point mutation. J. Gen. Physiol. 114:1-12.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 1-12
    • Lin, Y.-W.1    Lin, C.-W.2    Chen, T.-Y.3
  • 27
    • 0031046341 scopus 로고    scopus 로고
    • Analysis of a protein region involved in permeation and gating of the voltage-gated Torpedo chloride channel ClC-0
    • Ludewig, U., T.J. Jentsch, and M. Pusch. 1997. Analysis of a protein region involved in permeation and gating of the voltage-gated Torpedo chloride channel ClC-0. J. Physiol. 498:691-702.
    • (1997) J. Physiol. , vol.498 , pp. 691-702
    • Ludewig, U.1    Jentsch, T.J.2    Pusch, M.3
  • 28
    • 0029743660 scopus 로고    scopus 로고
    • Two physically distinct pores in the dimeric ClC-0 chloride channel
    • Ludewig, U., M. Pusch, and T.J. Jentsch. 1996. Two physically distinct pores in the dimeric ClC-0 chloride channel. Nature. 383:340-343.
    • (1996) Nature , vol.383 , pp. 340-343
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 31
    • 0033873930 scopus 로고    scopus 로고
    • A decade of CLC chloride channels: Structure, mechanism, and many unsettled questions
    • Maduke, M., C. Miller, and J.A. Mindell. 2000. A decade of CLC chloride channels: structure, mechanism, and many unsettled questions. Annu. Rev. Biophys. Biomol. Struct. 29:411-438.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 411-438
    • Maduke, M.1    Miller, C.2    Mindell, J.A.3
  • 32
    • 0028102941 scopus 로고
    • Purification, reconstitution, and subunit composition of a voltage-gated chloride channel from Torpedo electroplax
    • Middleton, R.E., D.J. Pheasant, and C. Miller. 1994. Purification, reconstitution, and subunit composition of a voltage-gated chloride channel from Torpedo electroplax. Biochemistry. 33:13189-13198.
    • (1994) Biochemistry , vol.33 , pp. 13189-13198
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 33
    • 0029661878 scopus 로고    scopus 로고
    • Homodimeric architecture of a ClC-type chloride ion channel
    • Middleton, R.E., D.J. Pheasant, and C. Miller. 1996. Homodimeric architecture of a ClC-type chloride ion channel. Nature. 383:337-340.
    • (1996) Nature , vol.383 , pp. 337-340
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 34
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax
    • Miller, C. 1982. Open-state substructure of single chloride channels from Torpedo electroplax. Phil. Trans. R. Soc. Lond. B Biol. Sci. 299:401-411.
    • (1982) Phil. Trans. R. Soc. Lond. B Biol. Sci. , vol.299 , pp. 401-411
    • Miller, C.1
  • 35
    • 0002652291 scopus 로고
    • The Torpedo chloride channel: Intimations of molecular structure from quirks of single-channel function
    • A. Leefmans and J. Russel, editors. Plenum Press, New York
    • Miller, C., and E.A. Richard. 1990. The Torpedo chloride channel: intimations of molecular structure from quirks of single-channel function. In Chloride Transporters. A. Leefmans and J. Russel, editors. Plenum Press, New York. 383-405.
    • (1990) Chloride Transporters , pp. 383-405
    • Miller, C.1    Richard, E.A.2
  • 36
    • 0021180163 scopus 로고
    • Dimeric structure of single chloride channels from Torpedo electroplax
    • Miller, C., and M.M. White. 1984. Dimeric structure of single chloride channels from Torpedo electroplax. Proc. Natl. Acad. Sci. USA. 81:2772-2775.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2772-2775
    • Miller, C.1    White, M.M.2
  • 37
    • 0026054610 scopus 로고
    • The nucleotide sequence of a voltage-gated chloride channel from the electric organ of Torpedo californica
    • O'Neill, G.P., R. Grygorczyk, M. Adam, and A.W. Ford-Hutchinson. 1991. The nucleotide sequence of a voltage-gated chloride channel from the electric organ of Torpedo californica. Biochim. Biophys. Acta. 1129:131-134.
    • (1991) Biochim. Biophys. Acta , vol.1129 , pp. 131-134
    • O'Neill, G.P.1    Grygorczyk, R.2    Adam, M.3    Ford-Hutchinson, A.W.4
  • 38
    • 0025360783 scopus 로고
    • Modifications of single acetylcholine-activated channels in BC3H-1 cells
    • Pappone, P.A., and G.L. Barchfeld. 1990. Modifications of single acetylcholine-activated channels in BC3H-1 cells. J. Gen. Physiol. 96:1-22.
    • (1990) J. Gen. Physiol. , vol.96 , pp. 1-22
    • Pappone, P.A.1    Barchfeld, G.L.2
  • 39
    • 0034930508 scopus 로고    scopus 로고
    • Mechanism of block of single protopores of the Torpedo chloride channel ClC-0 by 2-(p-chlorophenoxy)butyric acid (CPB)
    • Pusch, M., A. Accardi, A. Liantonio, L. Ferrera, A. De Luca, D.Cq. Camerino, and F. Conti. 2001. Mechanism of block of single protopores of the Torpedo chloride channel ClC-0 by 2-(p-chlorophenoxy)butyric acid (CPB). J. Gen. Physiol. 118:45-62.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 45-62
    • Pusch, M.1    Accardi, A.2    Liantonio, A.3    Ferrera, L.4    De Luca, A.5    Camerino, D.Cq.6    Conti, F.7
  • 40
    • 0028924935 scopus 로고
    • Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion
    • Pusch, M., U. Ludewig, A. Rehfeldt, and T.J. Jentsch. 1995. Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion. Nature. 373:527-531.
    • (1995) Nature , vol.373 , pp. 527-531
    • Pusch, M.1    Ludewig, U.2    Rehfeldt, A.3    Jentsch, T.J.4
  • 41
    • 0041397940 scopus 로고
    • Activity coefficients of electrolytes at 25°C
    • Academic Press Inc., New York, NY. 477 pp
    • Robinson, R.A., and R.H. Stokes. 1955. Activity coefficients of electrolytes at 25°C. In Electrolyte Solutions. Academic Press Inc., New York, NY. 477 pp.
    • (1955) Electrolyte Solutions
    • Robinson, R.A.1    Stokes, R.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.