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Volumn 127, Issue 4, 2006, Pages 435-447

Roles of K149, G352, and H401 in the channel functions of ClC-0: Testing the predictions from theoretical calculations

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHLORIDE CHANNEL; LEUCINE; MEMBRANE PROTEIN;

EID: 33645304847     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200509460     Document Type: Article
Times cited : (17)

References (36)
  • 4
    • 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
  • 5
    • 4444366193 scopus 로고    scopus 로고
    • Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel
    • Bostick, D.L., and M.L. Berkowitz. 2004. Exterior site occupancy infers chloride-induced proton gating in a prokaryotic homolog of the ClC chloride channel. Biophys. J. 87:1686-1696.
    • (2004) Biophys. J. , vol.87 , pp. 1686-1696
    • Bostick, D.L.1    Berkowitz, M.L.2
  • 6
    • 0034940574 scopus 로고    scopus 로고
    • + of the muscle-type ClC chloride channels
    • + of the muscle-type ClC chloride channels. J. Gen. Physiol. 118:23-32.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 23-32
    • Chen, M.F.1    Chen, T.Y.2
  • 7
    • 0042377364 scopus 로고    scopus 로고
    • Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels
    • Chen, M.F., and T.Y. Chen. 2003. Side-chain charge effects and conductance determinants in the pore of ClC-0 chloride channels. J. Gen. Physiol. 122:133-145.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 133-145
    • Chen, M.F.1    Chen, T.Y.2
  • 8
    • 0032407783 scopus 로고    scopus 로고
    • Extracellular zinc ion inhibits ClC-0 chloride channels by facilitating slow gating
    • Chen, T.Y. 1998. Extracellular 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
  • 9
    • 15544388091 scopus 로고    scopus 로고
    • Structure and function of clc channels
    • Chen, T.Y. 2005. Structure and function of clc channels. Annu. Rev. Physiol. 67:809-839.
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 809-839
    • Chen, T.Y.1
  • 10
    • 0242415285 scopus 로고    scopus 로고
    • Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels
    • Chen, T.Y., M.F. Chen, and C.W. Lin. 2003. Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels. J. Gen. Physiol. 122:641-651.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 641-651
    • Chen, T.Y.1    Chen, M.F.2    Lin, C.W.3
  • 12
    • 1142291714 scopus 로고    scopus 로고
    • Mechanism of anionic conduction across ClC
    • Cohen, J., and K. Schulten. 2004. Mechanism of anionic conduction across ClC. Biophys. J. 86:836-845.
    • (2004) Biophys. J. , vol.86 , pp. 836-845
    • Cohen, J.1    Schulten, K.2
  • 13
    • 1142310688 scopus 로고    scopus 로고
    • Conduction mechanisms of chloride ions in ClC-type channels
    • Corry, B., M. O'Mara, and S.H. Chung. 2004. Conduction mechanisms of chloride ions in ClC-type channels. Biophys. J. 86:846-860.
    • (2004) Biophys. J. , vol.86 , pp. 846-860
    • Corry, B.1    O'Mara, M.2    Chung, S.H.3
  • 14
    • 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
  • 15
    • 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
  • 16
    • 22244489419 scopus 로고    scopus 로고
    • Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule
    • Engh, A.M., and M. Maduke. 2005. Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule. J. Gen. Physiol. 125:601-617.
    • (2005) J. Gen. Physiol. , vol.125 , pp. 601-617
    • Engh, A.M.1    Maduke, M.2
  • 17
    • 0345146920 scopus 로고    scopus 로고
    • Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1
    • Estevez, R., B.C. Schroeder, A. Accardi, T.J. Jentsch, and M. Pusch. 2003. Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1. Neuron. 38:47-59.
    • (2003) Neuron , vol.38 , pp. 47-59
    • Estevez, R.1    Schroeder, B.C.2    Accardi, A.3    Jentsch, T.J.4    Pusch, M.5
  • 18
    • 2542437774 scopus 로고    scopus 로고
    • Electrostatics of ion stabilization in a ClC chloride channel homologue from Escherichia coli
    • Faraldo-Gomez, J.D., and B. Roux. 2004. Electrostatics of ion stabilization in a ClC chloride channel homologue from Escherichia coli. J. Mol. Biol. 339:981-1000.
    • (2004) J. Mol. Biol. , vol.339 , pp. 981-1000
    • Faraldo-Gomez, J.D.1    Roux, B.2
  • 19
    • 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
  • 21
    • 0035022709 scopus 로고    scopus 로고
    • Scam feels the pinch
    • Karlin, A. 2001. Scam feels the pinch. J. Gen. Physiol. 117:235-238.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 235-238
    • Karlin, A.1
  • 22
    • 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
  • 23
    • 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. 122:147-159.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 147-159
    • Lin, C.W.1    Chen, T.Y.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 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
  • 28
    • 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. Philos. Trans. R. Soc. Lond. B Biol. Sci. 299:401-411.
    • (1982) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.299 , pp. 401-411
    • Miller, C.1
  • 29
    • 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
  • 30
    • 1142310684 scopus 로고    scopus 로고
    • - pores: Electrostatic effects of charged residues
    • - pores: electrostatic effects of charged residues. Biophys. J. 86:825-835.
    • (2004) Biophys. J. , vol.86 , pp. 825-835
    • Miloshevsky, G.V.1    Jordan, P.C.2
  • 31
    • 0031781630 scopus 로고    scopus 로고
    • State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor. Inferences from rates of reaction of thiosulfonates with substituted cysteines in the M2 segment of the α subunit
    • Pascual, J.M., and A. Karlin. 1998. State-dependent accessibility and electrostatic potential in the channel of the acetylcholine receptor. Inferences from rates of reaction of thiosulfonates with substituted cysteines in the M2 segment of the α subunit. J. Gen. Physiol. 111:717-739.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 717-739
    • Pascual, J.M.1    Karlin, A.2
  • 32
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • Picollo, A., and M. Pusch. 2005. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature. 436:420-423.
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 33
    • 15244340198 scopus 로고    scopus 로고
    • Unique structure and function of chloride transporting CLC proteins
    • Pusch, M., and T.J. Jentsch. 2005. Unique structure and function of chloride transporting CLC proteins. IEEE Trans Nanobioscience. 4:49-57.
    • (2005) IEEE Trans Nanobioscience , vol.4 , pp. 49-57
    • Pusch, M.1    Jentsch, T.J.2
  • 34
    • 0032921415 scopus 로고    scopus 로고
    • The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia
    • Saviane, C., F. Conti, and M. Pusch. 1999. The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia. J. Gen. Physiol. 113:457-468.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 457-468
    • Saviane, C.1    Conti, F.2    Pusch, M.3
  • 35
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • Scheel, O., A.A. Zdebik, S. Lourdel, and T.J. Jentsch. 2005. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature. 436:424-427.
    • (2005) Nature , vol.436 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 36
    • 0033813781 scopus 로고    scopus 로고
    • The intrinsic electrostatic potential and the intermediate ring of charge in the acetylcholine receptor channel
    • Wilson, G.G., J.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, J.M.2    Brooijmans, N.3    Murray, D.4    Karlin, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.