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Volumn 70, Issue 6, 1996, Pages 2688-2695

Identification of cystic fibrosis transmembrane conductance regulator channel-lining residues in and flanking the M6 membrane-spanning segment

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE CHANNEL; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0030051032     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79838-7     Document Type: Article
Times cited : (96)

References (61)
  • 1
    • 0028809730 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α-subunit
    • Akabas, M. H., and A. Karlin. 1995. Identification of acetylcholine receptor channel-lining residues in the M1 segment of the α-subunit. Biochemistry: 34:12496-12500.
    • (1995) Biochemistry , vol.34 , pp. 12496-12500
    • Akabas, M.H.1    Karlin, A.2
  • 2
    • 0027987062 scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the a subunit
    • Akabas, M. H., C. Kaufmann, P. Archdeacon, and A. Karlin. 1994a. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the a subunit. Neuron. 13:919-927.
    • (1994) Neuron , vol.13 , pp. 919-927
    • Akabas, M.H.1    Kaufmann, C.2    Archdeacon, P.3    Karlin, A.4
  • 3
    • 0028264188 scopus 로고
    • Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator
    • Akabas, M. H., C. Kaufmann, T. A. Cook, and P. Archdeacon. 1994b. Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator, J. Biol. Chem. 269: 14865-14868.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14865-14868
    • Akabas, M.H.1    Kaufmann, C.2    Cook, T.A.3    Archdeacon, P.4
  • 4
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M. H., D. A. Stauffer, M. Xu, and A. Karlin. 1992, Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science. 258:307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 5
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach, C., T. Marti, H. G. Khorana, and W. L. Hubbell. 1990. Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science. 248:1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 6
    • 0026472873 scopus 로고
    • Traffic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames, G. F-L., C. S. Mimura, S. R. Holbrook, and V. Shyamala. 1992. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv. Enzymol. 65:1-47.
    • (1992) Adv. Enzymol. , vol.65 , pp. 1-47
    • Ames, G.F.-L.1    Mimura, C.S.2    Holbrook, S.R.3    Shyamala, V.4
  • 7
    • 0025931429 scopus 로고
    • Nucleotide triphosphates are required to open the CFTR chloride channel
    • Anderson, M. P., H. A. Berger, D. P. Rich, R. J. Gregory, A. E. Smith, and M. J. Welsh. 1991a. Nucleotide triphosphates are required to open the CFTR chloride channel. Cell 67:775-784.
    • (1991) Cell , vol.67 , pp. 775-784
    • Anderson, M.P.1    Berger, H.A.2    Rich, D.P.3    Gregory, R.J.4    Smith, A.E.5    Welsh, M.J.6
  • 10
    • 0028174962 scopus 로고
    • Coupling of CFTR CP channel gating to an ATP hydrolysis cycle
    • Baukrowitz, T., T.-C. Hwang, A. C. Nairn, and D. C. Gadsby. 1994. Coupling of CFTR CP channel gating to an ATP hydrolysis cycle. Neuron. 12:473-482.
    • (1994) Neuron , vol.12 , pp. 473-482
    • Baukrowitz, T.1    Hwang, T.-C.2    Nairn, A.C.3    Gadsby, D.C.4
  • 12
    • 0027519153 scopus 로고
    • Regulation of the cystic fibrosis transmembrane conductance regulator CP channel by specific protein kinases and protein phosphatases
    • Berger, H. A., S. M. Travis, and M. J. Welsh. 1993. Regulation of the cystic fibrosis transmembrane conductance regulator CP channel by specific protein kinases and protein phosphatases. J. Biol Chem. 268: 2037-2047.
    • (1993) J. Biol Chem. , vol.268 , pp. 2037-2047
    • Berger, H.A.1    Travis, S.M.2    Welsh, M.J.3
  • 13
    • 0028906612 scopus 로고
    • The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity
    • Carson, M. R., S. M. Travis, and M. J. Welsh. 1995. The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity. J. Biol. Chem. 270:1711-1717.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1711-1717
    • Carson, M.R.1    Travis, S.M.2    Welsh, M.J.3
  • 14
    • 0028241858 scopus 로고
    • Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion
    • Chang, X. B., Y. X. Hou, T. J. Jensen, and J. R. Riordan. 1994. Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion. J. Biol. Chem. 269:18572-18575.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18572-18575
    • Chang, X.B.1    Hou, Y.X.2    Jensen, T.J.3    Riordan, J.R.4
  • 15
    • 0027311276 scopus 로고
    • Protein kinase a (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites
    • Chang, X-B., J. A. Tabcharam, Y.-X. Hou, T. J. Jensen, N. Kartner, N. Alon, J. W. Hanrahan, and J. R. Riordan. 1993. Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites. J. Biol. Chem. 268:11304-11311.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11304-11311
    • Chang, X.-B.1    Tabcharam, J.A.2    Hou, Y.-X.3    Jensen, T.J.4    Kartner, N.5    Alon, N.6    Hanrahan, J.W.7    Riordan, J.R.8
  • 16
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • Cheng, S. H., D. P. Rich, J. Marshall, R. J. Gregory, M. J. Welsh, and A. E. Smith. 1991. Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell. 66: 1027-1036.
    • (1991) Cell , vol.66 , pp. 1027-1036
    • Cheng, S.H.1    Rich, D.P.2    Marshall, J.3    Gregory, R.J.4    Welsh, M.J.5    Smith, A.E.6
  • 19
    • 0025312731 scopus 로고
    • Multiple mutations in highly conserved residues are found in mildly affected cystic fibrosis patients
    • Dean, M., M. B. White, J. Amos, B. Gerrard, C. Steward, K. T. Khaw, and M. Leppert. 1990. Multiple mutations in highly conserved residues are found in mildly affected cystic fibrosis patients. Cell. 61:863-870.
    • (1990) Cell , vol.61 , pp. 863-870
    • Dean, M.1    White, M.B.2    Amos, J.3    Gerrard, B.4    Steward, C.5    Khaw, K.T.6    Leppert, M.7
  • 21
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M. M., and I. Pastan. 1993. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem. 62: 385-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 23
    • 0029117303 scopus 로고
    • Conformational states of CFTR associated with channel gating: The role of ATP binding and hydrolysis
    • Gunderson, K. L., and R. R. Kopito. 1995. Conformational states of CFTR associated with channel gating: the role of ATP binding and hydrolysis. Cell. 82:231-239.
    • (1995) Cell , vol.82 , pp. 231-239
    • Gunderson, K.L.1    Kopito, R.R.2
  • 25
    • 0029001515 scopus 로고
    • Generation, translocation and presentation of MHC class I-restricted peptides
    • Heemels, M. T., and H. Ploegh. 1995. Generation, translocation and presentation of MHC class I-restricted peptides. Annu. Rev. Biochem. 64:463-492.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 463-492
    • Heemels, M.T.1    Ploegh, H.2
  • 26
    • 0028596211 scopus 로고
    • N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann, M., C. Maron, and S. Heinemann. 1994. N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron. 13:1331-1343.
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 28
    • 0028340159 scopus 로고
    • Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis
    • Hwang, T. C., G. Nagel, A. C. Nairn, and D. C. Gadsby. 1994. Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis. Proc. Nail. Acad. Sci. USA. 91:4698-4702.
    • (1994) Proc. Nail. Acad. Sci. USA , vol.91 , pp. 4698-4702
    • Hwang, T.C.1    Nagel, G.2    Nairn, A.C.3    Gadsby, D.C.4
  • 29
    • 0028920298 scopus 로고
    • Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method
    • Javitch, J. A., D. Fu, J. Chen, and A. Karlin. 1995. Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method. Neuron. 14:825-831.
    • (1995) Neuron , vol.14 , pp. 825-831
    • Javitch, J.A.1    Fu, D.2    Chen, J.3    Karlin, A.4
  • 30
    • 0027375714 scopus 로고
    • Use of site-directed fluorescence labelling to study proximity relationships in the lactose permease of Escherichia coli
    • Jung, K., H. Jung, J. Wu, G. G. Prive, and H. R. Kaback. 1993. Use of site-directed fluorescence labelling to study proximity relationships in the lactose permease of Escherichia coli. Biochemistry. 32: 12273-12278.
    • (1993) Biochemistry , vol.32 , pp. 12273-12278
    • Jung, K.1    Jung, H.2    Wu, J.3    Prive, G.G.4    Kaback, H.R.5
  • 31
    • 0028941130 scopus 로고
    • + channel probed by sulfhydryl-specific reagents after scanning-cysteine mutagenesis
    • + channel probed by sulfhydryl-specific reagents after scanning-cysteine mutagenesis. Biophys. J. 68:900-905.
    • (1995) Biophys. J. , vol.68 , pp. 900-905
    • Kurz, L.L.1    Zuhlke, R.D.2    Zhang, H.J.3    Joho, R.H.4
  • 32
    • 0028960949 scopus 로고
    • Silver as a probe of pore-forming residues in a potassium channel
    • Lu, Q., and C. Miller. 1995. Silver as a probe of pore-forming residues in a potassium channel. Science. 268:304-307.
    • (1995) Science , vol.268 , pp. 304-307
    • Lu, Q.1    Miller, C.2
  • 33
    • 0029012475 scopus 로고
    • Pore loops: An emerging theme in ion channel structure
    • MacKinnon, R. 1995. Pore loops: an emerging theme in ion channel structure. Neuron. 14:889-892.
    • (1995) Neuron , vol.14 , pp. 889-892
    • MacKinnon, R.1
  • 34
    • 0028111941 scopus 로고
    • Novel pore-lining residues in CFTR that govern permeation and openchannel block
    • McDonough, S., N. Davidson, H. A. Lester, and N. A. McCarty. 1994. Novel pore-lining residues in CFTR that govern permeation and openchannel block. Neuron. 13:623-634.
    • (1994) Neuron , vol.13 , pp. 623-634
    • McDonough, S.1    Davidson, N.2    Lester, H.A.3    McCarty, N.A.4
  • 35
    • 0028235219 scopus 로고
    • Reaction of diphtheria toxin channels with sulfhydryl-specific reagents: Observation of chemical reactions at the single molecule level
    • Mindell, J. A., H. Zhan, P. D. Huynh, R. J. Collier, and A. Finkelstein. 1994. Reaction of diphtheria toxin channels with sulfhydryl-specific reagents: observation of chemical reactions at the single molecule level. Proc. Natl. Acad. Sci. USA. 91:5272-5276.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5272-5276
    • Mindell, J.A.1    Zhan, H.2    Huynh, P.D.3    Collier, R.J.4    Finkelstein, A.5
  • 37
    • 0029070117 scopus 로고
    • + pore structure revealed by reporter cysteines at inner and outer surfaces
    • + pore structure revealed by reporter cysteines at inner and outer surfaces. Neuron. 14:1055-1063.
    • (1995) Neuron , vol.14 , pp. 1055-1063
    • Pascual, J.M.1    Shieh, C.C.2    Kirsch, G.E.3    Brown, A.M.4
  • 40
    • 0023055733 scopus 로고
    • Reactivity of small thiolate anions and cysteine-25 in papain towards methyl-methanethiosulfonate
    • Roberts, D. D., S. D. Lewis, D. P. Ballou, S. T. Olson, and J. A. Shafer. 1986. Reactivity of small thiolate anions and cysteine-25 in papain towards methyl-methanethiosulfonate. Biochemistry. 25:5595-5601.
    • (1986) Biochemistry , vol.25 , pp. 5595-5601
    • Roberts, D.D.1    Lewis, S.D.2    Ballou, D.P.3    Olson, S.T.4    Shafer, J.A.5
  • 41
    • 0027330222 scopus 로고
    • Two novel mutations in the transmembrane domains of the CFTR gene in subjects of Sardinian descent
    • Saba, L., G. B. Leoni, A. Meloni, V. Faà, A. Cao, and M. C. Rosatilli. 1993. Two novel mutations in the transmembrane domains of the CFTR gene in subjects of Sardinian descent. Hum. Mol. Genet. 2:1739-1740.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1739-1740
    • Saba, L.1    Leoni, G.B.2    Meloni, A.3    Faà, V.4    Cao, A.5    Rosatilli, M.C.6
  • 42
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channel at 3.1 Å resolution
    • Schirmer, T., T. A. Keller, Y.-F. Wang, and J. P. Rosenbusch. 1995. Structural basis for sugar translocation through maltoporin channel at 3.1 Å resolution. Nature. 267:512-514.
    • (1995) Nature , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.-F.3    Rosenbusch, J.P.4
  • 44
    • 0028980536 scopus 로고
    • CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP
    • Schwiebert, E. M., M. E. Egan, T. H. Hwang, S. B. Fulmer, S. A. Allen, G. R. Cutting, and W. B. Guggino. 1995. CFTR regulates outwardly rectifying chloride channels through an autocrine mechanism involving ATP. Cell. 81:1063-1073.
    • (1995) Cell , vol.81 , pp. 1063-1073
    • Schwiebert, E.M.1    Egan, M.E.2    Hwang, T.H.3    Fulmer, S.B.4    Allen, S.A.5    Cutting, G.R.6    Guggino, W.B.7
  • 45
    • 0028906638 scopus 로고
    • cAMP-dependent protein kinase-mediated phosphorylation of cystic fibrosis transmembrane conductance regulator residue Ser-753 and its role in channel activation
    • Seibert, F. S., J. A. Tabcharani, X. B. Chang, A. M. Dulhanty, C. Mathews, J. W. Hanrahan, and J. R. Riordan. 1995. cAMP-dependent protein kinase-mediated phosphorylation of cystic fibrosis transmembrane conductance regulator residue Ser-753 and its role in channel activation. J Biol. Chem. 270:2158-2162.
    • (1995) J Biol. Chem. , vol.270 , pp. 2158-2162
    • Seibert, F.S.1    Tabcharani, J.A.2    Chang, X.B.3    Dulhanty, A.M.4    Mathews, C.5    Hanrahan, J.W.6    Riordan, J.R.7
  • 47
    • 0028100898 scopus 로고
    • Identification of a translocated protein segment in a voltage-dependent channel
    • Slatin, S. L., X. Q. Qiu, K. S. Jakes, and A. Finkelstein. 1994. Identification of a translocated protein segment in a voltage-dependent channel. Nature. 371:158-161.
    • (1994) Nature , vol.371 , pp. 158-161
    • Slatin, S.L.1    Qiu, X.Q.2    Jakes, K.S.3    Finkelstein, A.4
  • 48
    • 0027364318 scopus 로고
    • Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator
    • Smit, L. S., D. J. Wilkinson, M. K. Mansoura, F. S. Collins, and D. C. Dawson. 1993. Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator. Proc. Natl. Acad. Sci. USA. 90:9963-9967.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9963-9967
    • Smit, L.S.1    Wilkinson, D.J.2    Mansoura, M.K.3    Collins, F.S.4    Dawson, D.C.5
  • 49
    • 0028355745 scopus 로고
    • Electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates
    • Stauffer, D. A., and A. Karlin. 1994. Electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates. Biochemistry. 33:6840-6849.
    • (1994) Biochemistry , vol.33 , pp. 6840-6849
    • Stauffer, D.A.1    Karlin, A.2
  • 51
    • 0030057048 scopus 로고    scopus 로고
    • Exposure of residues in the cyclic-nucleotide-gated channel pore: P region structure and function in gating
    • Sun, Z. P., M. H. Akabas, E. H. Goulding, A. Karlin, and S. A. Siegelbaum. 1996. Exposure of residues in the cyclic-nucleotide-gated channel pore: P region structure and function in gating. Neuron. 16:141-149.
    • (1996) Neuron , vol.16 , pp. 141-149
    • Sun, Z.P.1    Akabas, M.H.2    Goulding, E.H.3    Karlin, A.4    Siegelbaum, S.A.5
  • 54
    • 0024809884 scopus 로고
    • Site-directed mutagenesis of colicin El provides specific attachment sites for spin labels whose spectra are sensitive to local conformation
    • Todd, A. P., J. Cong, F. Levinthal, C. Levinthal, and W. L. Hubbell. 1989. Site-directed mutagenesis of colicin El provides specific attachment sites for spin labels whose spectra are sensitive to local conformation. Proteins. 6:294-305.
    • (1989) Proteins , vol.6 , pp. 294-305
    • Todd, A.P.1    Cong, J.2    Levinthal, F.3    Levinthal, C.4    Hubbell, W.L.5
  • 55
    • 0027179469 scopus 로고
    • Interaction of nucleotides with membrane-associated cystic fibrosis transmembrane conductance regulator
    • Travis, S. M., M. R. Carson, D. R. Ries, and M. J. Welsh. 1993. Interaction of nucleotides with membrane-associated cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 268:15336-15339.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15336-15339
    • Travis, S.M.1    Carson, M.R.2    Ries, D.R.3    Welsh, M.J.4
  • 56
    • 0027034365 scopus 로고
    • Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: A report from the cystic fibrosis genetic analysis consortium
    • Tsui, L-C. 1992. Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: a report from the cystic fibrosis genetic analysis consortium. Hum. Mutat. 1:197-203.
    • (1992) Hum. Mutat. , vol.1 , pp. 197-203
    • Tsui, L.-C.1
  • 57
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss, M. S. U. Abele, J. Weckesser, W. Welte, E. Schiltz, and G. E. Schulz. 1991. Molecular architecture and electrostatic properties of a bacterial porin. Science. 254:1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.1    Abele, S.U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 59
    • 0027501362 scopus 로고
    • Amino acids lining the channel of the γ-aminobutyric acid type A receptor identified by cysteine substitution
    • Xu, M., and M. H. Akabas. 1993. Amino acids lining the channel of the γ-aminobutyric acid type A receptor identified by cysteine substitution. J. Biol. Chem. 268:21505-21508.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21505-21508
    • Xu, M.1    Akabas, M.H.2
  • 61
    • 0028970548 scopus 로고
    • Interaction of picrotoxin with GABAA receptor channel-lining residues probed in cysteine mutants
    • Xu, M., D. F. Covey, and M. H. Akabas. 1995. Interaction of picrotoxin with GABAA 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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