메뉴 건너뛰기




Volumn 375, Issue 3, 2003, Pages 633-641

Stable dimeric assembly of the second membrane-spanning domain of CFTR (cystic fibrosis transmembrane conductance regulator) reconstitutes a chloride-selective pore

Author keywords

Chloride selective channel; Cysteine modification; Cystic fibrosis transmembrane conductance regulator (CFTR); Dimer; Glycosylation; Second membrane spanning domain

Indexed keywords

BIOLOGICAL MEMBRANES; CHLORIDE MINERALS; DIMERS; FLUXES; NEGATIVE IONS; PROTEINS;

EID: 0242637061     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030774     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 0029436976 scopus 로고
    • Cystic fibrosis
    • Welsh, M. J. and Smith, A. E. (1995) Cystic fibrosis. Sci. Am. 273, 52-59
    • (1995) Sci. Am. , vol.273 , pp. 52-59
    • Welsh, M.J.1    Smith, A.E.2
  • 2
    • 1842333889 scopus 로고    scopus 로고
    • Genotype and phenotype in cystic fibrosis
    • Off. Ed.
    • Tsui, L. C. and Durie, P. (1997) Genotype and phenotype in cystic fibrosis. Hosp. Pract. (Off. Ed.) 32, 115-118, 123-129, 134
    • (1997) Hosp. Pract. , vol.32 , pp. 115-118
    • Tsui, L.C.1    Durie, P.2
  • 4
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G. and Roth, C. B. (2001) Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293, 1793-1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 5
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T. and Rees, D. C. (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 6
    • 0034084793 scopus 로고    scopus 로고
    • Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore
    • Linsdell, P., Evagelidis, A. and Hanrahan, J. W. (2000) Molecular determinants of anion selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel pore. Biophys. J. 78, 2973-2982
    • (2000) Biophys. J. , vol.78 , pp. 2973-2982
    • Linsdell, P.1    Evagelidis, A.2    Hanrahan, J.W.3
  • 7
    • 0032912589 scopus 로고    scopus 로고
    • Structure and function of the CFTR chloride channel
    • Sheppard, D. N. and Welsh, M. J. (1999) Structure and function of the CFTR chloride channel. Physiol. Rev. 79 (Suppl. 1), S23-S45
    • (1999) Physiol. Rev. , vol.79 , Issue.1 SUPPL.
    • Sheppard, D.N.1    Welsh, M.J.2
  • 8
    • 0029861859 scopus 로고    scopus 로고
    • - channels expressed in a mammalian cell line and its regulation by a critical pore residue
    • Cambridge, U.K.
    • - channels expressed in a mammalian cell line and its regulation by a critical pore residue. J. Physiol. (Cambridge, U.K.) 496, 687-693
    • (1996) J. Physiol. , vol.496 , pp. 687-693
    • Linsdell, P.1    Hanrahan, J.W.2
  • 10
    • 0030964656 scopus 로고    scopus 로고
    • Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels
    • Tabcharani, J. A., Linsdell, P. and Hanrahan, J. W. (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
  • 11
    • 0030885564 scopus 로고    scopus 로고
    • Permeability of wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels to polyatomic anions
    • Linsdell, P., Tabcharani, J. A., Rommens, J. M., Hou, Y. X., Chang, X. B., Tsui, L. C., Riordan, J. R. and Hanrahan, J. W. (1997) Permeability of wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels to polyatomic anions. J. Gen. Physiol. 110, 355-364
    • (1997) J. Gen. Physiol. , vol.110 , pp. 355-364
    • Linsdell, P.1    Tabcharani, J.A.2    Rommens, J.M.3    Hou, Y.X.4    Chang, X.B.5    Tsui, L.C.6    Riordan, J.R.7    Hanrahan, J.W.8
  • 12
    • 0030886246 scopus 로고    scopus 로고
    • Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell, P. Tabcharani, J. A. and Hanrahan, J. W. (1997) Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 110, 365-377
    • (1997) J. Gen. Physiol. , vol.110 , pp. 365-377
    • Linsdell, P.1    Tabcharani, J.A.2    Hanrahan, J.W.3
  • 13
    • 0034774836 scopus 로고    scopus 로고
    • CFTR: Covalent and noncovalent modification suggests a role for fixed charges in anion conduction
    • Smith, S. S., Liu, X, Zhang, Z. R., Sun, F., Kriewall, T. E., McCarty, N. A. and Dawson, D. C. (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
  • 14
    • 0033608961 scopus 로고    scopus 로고
    • 352 is a major determinant of charge selectivity in the cystic fibrosis transmembrane conductance regulator chloride channel
    • 352 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
  • 15
    • 0030893916 scopus 로고    scopus 로고
    • Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel
    • Cheung, M. and Akabas, M. H. (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
  • 17
    • 0038120974 scopus 로고    scopus 로고
    • Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore
    • Cambridge, U.K.
    • Gong, X. and Linsdell, P. (2003) Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride channel pore. J. Physiol. (Cambridge, U.K.) 549, 387-391
    • (2003) J. Physiol. , vol.549 , pp. 387-391
    • Gong, X.1    Linsdell, P.2
  • 18
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and open-channel block
    • Donough, S., Davidson, M., Lester, H. A. and McCarty, N. A. (1994) Novel pore-lining residues in CFTR that govern permeation and open-channel block. Neuron 13, 623-634
    • (1994) Neuron , vol.13 , pp. 623-634
    • Donough, S.1    Davidson, M.2    Lester, H.A.3    McCarty, N.A.4
  • 20
    • 0035847135 scopus 로고    scopus 로고
    • - channel by butyrate and phenylbutyrate
    • - channel by butyrate and phenylbutyrate. Eur. J. Pharmacol. 411, 255-260
    • (2001) Eur. J. Pharmacol. , vol.411 , pp. 255-260
    • Linsdell, P.1
  • 22
    • 0032491516 scopus 로고    scopus 로고
    • The second half of the cystic fibrosis transmembrane conductance regulator forms a functional chloride channel
    • Devidas, S., Yue, H. and Guggino, W. B. (1998) The second half of the cystic fibrosis transmembrane conductance regulator forms a functional chloride channel. J. Biol. Chem. 273, 29373-29380
    • (1998) J. Biol. Chem. , vol.273 , pp. 29373-29380
    • Devidas, S.1    Yue, H.2    Guggino, W.B.3
  • 23
    • 0035811064 scopus 로고    scopus 로고
    • Asymmetric structure of the cystic fibrosis transmembrane conductance regulator chloride channel pore suggested by mutagenesis of the twelfth transmembrane region
    • Gupta, J., Evagelidis, A., Hanrahan, J. W. and Linsdell, P. (2001) Asymmetric structure of the cystic fibrosis transmembrane conductance regulator chloride channel pore suggested by mutagenesis of the twelfth transmembrane region. Biochemistry 40, 6620-6627
    • (2001) Biochemistry , vol.40 , pp. 6620-6627
    • Gupta, J.1    Evagelidis, A.2    Hanrahan, J.W.3    Linsdell, P.4
  • 24
    • 0033931302 scopus 로고    scopus 로고
    • Interaction between permeation and gating in a putative pore domain mutant in the cystic fibrosis transmembrane conductance regulator
    • Zhang, Z. R., McDonough, S. I. and McCarty, N. A. (2000) Interaction between permeation and gating in a putative pore domain mutant in the cystic fibrosis transmembrane conductance regulator. Biophys. J. 79, 298-313
    • (2000) Biophys. J. , vol.79 , pp. 298-313
    • Zhang, Z.R.1    McDonough, S.I.2    McCarty, N.A.3
  • 25
    • 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
  • 26
    • 0035807019 scopus 로고    scopus 로고
    • A monomer is the minimum functional unit required for channel and ATPase activity of the cystic fibrosis transmembrane conductance regulator
    • Ramjeesingh, M., Li, C., Kogan, I., Wang, Y., Huan, L. J. and Bear, C. E. (2001) A monomer is the minimum functional unit required for channel and ATPase activity of the cystic fibrosis transmembrane conductance regulator. Biochemistry 40, 10700-10706
    • (2001) Biochemistry , vol.40 , pp. 10700-10706
    • Ramjeesingh, M.1    Li, C.2    Kogan, I.3    Wang, Y.4    Huan, L.J.5    Bear, C.E.6
  • 28
    • 0002476741 scopus 로고
    • Silver-staining of proteins in polyacrylamide gels: General overview
    • 27a Rabilloud, T., Vuillard, L., Gilly, C. and Lawrence, J. J. (1994) Silver-staining of proteins in polyacrylamide gels: general overview. Cell. Mol. Biol. 40, 57-75
    • (1994) Cell. Mol. Biol. , vol.40 , pp. 57-75
    • Rabilloud, T.1    Vuillard, L.2    Gilly, C.3    Lawrence, J.J.4
  • 29
    • 0017613512 scopus 로고
    • Simplification of the protein assay method of Lowry et al. which is more generally applicable
    • 27b Peterson, G. L. (1977) Simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83, 346-356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 30
    • 0026066416 scopus 로고
    • Solubilization and functional reconstitution of a chloride channel from Torpedo California electroplax
    • Goldberg, A. F. and Miller, C. (1991) Solubilization and functional reconstitution of a chloride channel from Torpedo California electroplax. J. Membr. Biol. 124, 199-206
    • (1991) J. Membr. Biol. , vol.124 , pp. 199-206
    • Goldberg, A.F.1    Miller, C.2
  • 31
    • 0032568845 scopus 로고    scopus 로고
    • Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues
    • Long, J. C., Wang, S. and Vik, S. B. (1998) Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues. J. Biol. Chem. 273, 16235-16240
    • (1998) J. Biol. Chem. , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 32
    • 0024007567 scopus 로고
    • Biocytin hydrazide - A selective label for sialic acids, galactose, and other sugars in glycoconjugates using avidin-biotin technology
    • Bayer, E. A., Ben-Hur, H. and Wilchek, M. (1988) Biocytin hydrazide - a selective label for sialic acids, galactose, and other sugars in glycoconjugates using avidin-biotin technology. Anal. Biochem. 170, 271-281
    • (1988) Anal. Biochem. , vol.170 , pp. 271-281
    • Bayer, E.A.1    Ben-Hur, H.2    Wilchek, M.3
  • 33
    • 0033652948 scopus 로고    scopus 로고
    • Characterization of the oligosaccharide structures associated with the cystic fibrosis transmembrane conductance regulator
    • O'Riordan, C. R., Lachapelle, A. L., Marshall, J., Higgins, E. A. and Cheng, S. H. (2000) Characterization of the oligosaccharide structures associated with the cystic fibrosis transmembrane conductance regulator. Glycobiology 10, 1225-1233
    • (2000) Glycobiology , vol.10 , pp. 1225-1233
    • O'Riordan, C.R.1    Lachapelle, A.L.2    Marshall, J.3    Higgins, E.A.4    Cheng, S.H.5
  • 34
    • 0034435098 scopus 로고    scopus 로고
    • A novel CFTR disease-associated mutation causes addition of an extra N-linked oligosaccharide
    • Hammerle, M. M., Aleksandrov, A. A., Chang, X. B. and Riordan, J. R. (2000) A novel CFTR disease-associated mutation causes addition of an extra N-linked oligosaccharide. Glycoconj. J. 17, 807-813
    • (2000) Glycoconj. J. , vol.17 , pp. 807-813
    • Hammerle, M.M.1    Aleksandrov, A.A.2    Chang, X.B.3    Riordan, J.R.4
  • 35
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic CIC-type chloride channel
    • Maduke, M., Pheasant, D. J. and Miller, C. (1999) High-level expression, functional reconstitution, and quaternary structure of a prokaryotic CIC-type chloride channel. J. Gen. Physiol. 114, 713-722
    • (1999) J. Gen. Physiol. , vol.114 , pp. 713-722
    • Maduke, M.1    Pheasant, D.J.2    Miller, C.3
  • 36
    • 0026629383 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator chloride channel. Iodide block and permeation
    • Tabcharani, J. A., Chang, X. B., Riordan, J. R. and Hanrahan, J. W. (1992) The cystic fibrosis transmembrane conductance regulator chloride channel. Iodide block and permeation. Biophys. J. 62, 1-4
    • (1992) Biophys. J. , vol.62 , pp. 1-4
    • Tabcharani, J.A.1    Chang, X.B.2    Riordan, J.R.3    Hanrahan, J.W.4
  • 37
    • 0016787657 scopus 로고
    • Chemical modification of bovine heart mitochondrial malate dehydrogenase. Selective modification of cysteine and histidine
    • Gregory, E. M. (1975) Chemical modification of bovine heart mitochondrial malate dehydrogenase. Selective modification of cysteine and histidine. J. Biol. Chem. 250, 5470-5474
    • (1975) J. Biol. Chem. , vol.250 , pp. 5470-5474
    • Gregory, E.M.1
  • 38
    • 0030774895 scopus 로고    scopus 로고
    • Covalent modification of the regulatory domain irreversibly stimulates cystic fibrosis transmembrane conductance regulator
    • Gotten, J. F. and Welsh, M. J. (1997) Covalent modification of the regulatory domain irreversibly stimulates cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 272, 25617-25622
    • (1997) J. Biol. Chem. , vol.272 , pp. 25617-25622
    • Gotten, J.F.1    Welsh, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.