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Volumn 128, Issue 5, 2006, Pages 535-545

Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANION; ARGININE DERIVATIVE; CHLORIDE; CHLORIDE CHANNEL; CYSTEINE; ION; MUTANT PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 33750530196     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200609516     Document Type: Article
Times cited : (66)

References (32)
  • 2
    • 0041806510 scopus 로고    scopus 로고
    • A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification
    • Brelidze, T.I., X. Niu, and K.L. Magleby. 2003. A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification. Proc. Natl. Acad. Sci. USA. 100:9017-9022.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9017-9022
    • Brelidze, T.I.1    Niu, X.2    Magleby, K.L.3
  • 4
    • 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
  • 5
    • 0030893916 scopus 로고    scopus 로고
    • Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel
    • Cheung, M., and M.H. Akabas. 1997. Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. J. Gen. Physiol. 109:289-299.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 289-299
    • Cheung, M.1    Akabas, M.H.2
  • 6
    • 0033605158 scopus 로고    scopus 로고
    • Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge
    • Cotten, J.F., and M.J. Welsh. 1999. Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge. J. Biol. Chem. 274:5429-5435.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5429-5435
    • Cotten, J.F.1    Welsh, M.J.2
  • 7
    • 18544375165 scopus 로고    scopus 로고
    • Conduction through the inward rectifier potassium channel, Kir2.1, is increased by negatively charged extracellular residues
    • D'Avanzo, N., H.C. Cho, I. Tolokh, R. Pekhletski, I. Tolokh, C. Gray, S. Goldman, and P. Backx. 2005. Conduction through the inward rectifier potassium channel, Kir2.1, is increased by negatively charged extracellular residues. J. Gen. Physiol. 125:493-503.
    • (2005) J. Gen. Physiol. , vol.125 , pp. 493-503
    • D'Avanzo, N.1    Cho, H.C.2    Tolokh, I.3    Pekhletski, R.4    Tolokh, I.5    Gray, C.6    Goldman, S.7    Backx, P.8
  • 9
    • 0032232313 scopus 로고    scopus 로고
    • Topological model of membrane domain of the cystic fibrosis transmembrane conductance regulator
    • Gallet, X., F. Festy, P. Ducarme, R. Brasseur, and A. Thomas-Soumarmon. 1998. Topological model of membrane domain of the cystic fibrosis transmembrane conductance regulator. J. Mol. Graph. Model. 16:72-82.
    • (1998) J. Mol. Graph. Model. , vol.16 , pp. 72-82
    • Gallet, X.1    Festy, F.2    Ducarme, P.3    Brasseur, R.4    Thomas-Soumarmon, A.5
  • 10
    • 11244339684 scopus 로고    scopus 로고
    • Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Ge, N., C.N. Muise, X. Gong, and P. Linsdell. 2004. Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore. J. Biol. Chem. 279:55283-55289.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55283-55289
    • Ge, N.1    Muise, C.N.2    Gong, X.3    Linsdell, P.4
  • 11
    • 0344304517 scopus 로고    scopus 로고
    • Mutation-induced blocker permeability and multiion block of the CFTR chloride channel pore
    • Gong, X., and P. Linsdell. 2003a. Mutation-induced blocker permeability and multiion block of the CFTR chloride channel pore. J. Gen. Physiol. 122:673-687.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 673-687
    • Gong, X.1    Linsdell, P.2
  • 12
    • 0038120974 scopus 로고    scopus 로고
    • Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore
    • Gong, X., and P. Linsdell. 2003b. Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore. J. Physiol. 549:387-397.
    • (2003) J. Physiol. , vol.549 , pp. 387-397
    • Gong, X.1    Linsdell, P.2
  • 14
    • 0026026676 scopus 로고
    • Surface charges and ion channel function
    • Green, W.N., and O.S. Andersen. 1991. Surface charges and ion channel function. Annu. Rev. Physiol. 53:341-359.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 341-359
    • Green, W.N.1    Andersen, O.S.2
  • 15
    • 0033608961 scopus 로고    scopus 로고
    • Arg352 is a major determinant of charge selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Guinamard, R., and M.H. Akabas. 1999. Arg352 is a major determinant of charge selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel. Biochemistry. 38:5528-5537.
    • (1999) Biochemistry , vol.38 , pp. 5528-5537
    • Guinamard, R.1    Akabas, M.H.2
  • 18
    • 15744390354 scopus 로고    scopus 로고
    • Location of a common inhibitor binding site in the cytoplasmic vestibule of the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Linsdell, P. 2005. Location of a common inhibitor binding site in the cytoplasmic vestibule of the cystic fibrosis transmembrane conductance regulator chloride channel pore. J. Biol. Chem. 280:8945-8950.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8945-8950
    • Linsdell, P.1
  • 19
    • 32544435783 scopus 로고    scopus 로고
    • Mechanism of chloride permeation in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell, P. 2006. Mechanism of chloride permeation in the cystic fibrosis transmembrane conductance regulator chloride channel. Exp. Physiol. 91:123-129.
    • (2006) Exp. Physiol. , vol.91 , pp. 123-129
    • Linsdell, P.1
  • 20
    • 0029861859 scopus 로고    scopus 로고
    • - channels expressed in a mammalian cell line and its regulation by a critical pore residue
    • - channels expressed in a mammalian cell line and its regulation by a critical pore residue. J. Physiol. 496:687-693.
    • (1996) J. Physiol. , vol.496 , pp. 687-693
    • Linsdell, P.1    Hanrahan, J.W.2
  • 21
    • 0031954021 scopus 로고    scopus 로고
    • Adenosine triphosphate-dependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell, P., and J.W. Hanrahan. 1998. Adenosine triphosphate-dependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 111:601-614.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 601-614
    • Linsdell, P.1    Hanrahan, J.W.2
  • 24
    • 0033898228 scopus 로고    scopus 로고
    • Permeation through the CFTR chloride channel
    • McCarty, N.A. 2000. Permeation through the CFTR chloride channel. J. Exp. Biol. 203:1947-1962.
    • (2000) J. Exp. Biol. , vol.203 , pp. 1947-1962
    • McCarty, N.A.1
  • 25
    • 0035999832 scopus 로고    scopus 로고
    • Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels
    • Moorhouse, A.J., A. Keramidas, A. Zaykin, P.R. Schofield, and P.H. Barry. 2002. Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels. J. Gen. Physiol. 119:411-425.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 411-425
    • Moorhouse, A.J.1    Keramidas, A.2    Zaykin, A.3    Schofield, P.R.4    Barry, P.H.5
  • 26
    • 0043074453 scopus 로고    scopus 로고
    • Electrostatic tuning of ion conductance in potassium channels
    • Nimigean, C.M., J.S. Chappie, and C. Miller. 2003. Electrostatic tuning of ion conductance in potassium channels. Biochemistry. 42:9263-9268.
    • (2003) Biochemistry , vol.42 , pp. 9263-9268
    • Nimigean, C.M.1    Chappie, J.S.2    Miller, C.3
  • 28
    • 0029910820 scopus 로고    scopus 로고
    • Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity
    • Seibert, F.S., P. Linsdell, T.W. Loo, J.W. Hanrahan, J.R. Riordan, and D.M. Clarke. 1996. Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity. J. Biol. Chem. 271:27493-27499.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27493-27499
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Riordan, J.R.5    Clarke, D.M.6
  • 29
    • 0034774836 scopus 로고    scopus 로고
    • CFTR: Covalent and noncovalent modification suggests a role for fixed charges in anion conduction
    • Smith, S.S., X. Liu, Z.-R. Zhang, F. Sun, T.E. Kriewall, N.A. McCarty, and D.C. Dawson. 2001. CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction. J. Gen. Physiol. 118:407-431.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 407-431
    • Smith, S.S.1    Liu, X.2    Zhang, Z.-R.3    Sun, F.4    Kriewall, T.E.5    McCarty, N.A.6    Dawson, D.C.7
  • 30
    • 0030964656 scopus 로고    scopus 로고
    • Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels
    • Tabcharani, J.A., P. Linsdell, and J.W. Hanrahan. 1997. Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels. J. Gen. Physiol. 110:341-354.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 341-354
    • Tabcharani, J.A.1    Linsdell, P.2    Hanrahan, J.W.3
  • 31
    • 23244435078 scopus 로고    scopus 로고
    • Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor
    • Wang, Y., L. Xu, D.A. Pasek, D. Gillespie, and G. Meissner. 2005. Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor. Biophys. J. 89:256-265.
    • (2005) Biophys. J. , vol.89 , pp. 256-265
    • Wang, Y.1    Xu, L.2    Pasek, D.A.3    Gillespie, D.4    Meissner, G.5
  • 32
    • 0022599511 scopus 로고
    • Trimethyloxonium modification of single batrachotoxin-activated sodium channels in planar bilayers. Changes in unit conductance and in block by saxitoxin and calcium
    • Worley, J.F., R.J. French, and B.K. Krueger. 1986. Trimethyloxonium modification of single batrachotoxin-activated sodium channels in planar bilayers. Changes in unit conductance and in block by saxitoxin and calcium. J. Gen. Physiol. 87:327-349.
    • (1986) J. Gen. Physiol. , vol.87 , pp. 327-349
    • Worley, J.F.1    French, R.J.2    Krueger, B.K.3


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