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Volumn 271, Issue 2, 2000, Pages 518-525

ATP hydrolysis by a CFTR domain: Pharmacology and effects of G551D mutation

Author keywords

8 Cyclopentyl 1,3 dipropylxanthine; ABC transporter; ATP hydrolase; Flavonol; Vanadate

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE INHIBITOR; ADENOSINE TRIPHOSPHATE; CHLORIDE CHANNEL; GENISTEIN; GLIBENCLAMIDE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0034630742     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.2659     Document Type: Article
Times cited : (44)

References (53)
  • 2
    • 0032562143 scopus 로고    scopus 로고
    • Expression and characterization of the NBD1-R domain region of CFTR: Evidence for subunit-subunit interactions
    • Neville, D. C., Rozanas, C. R., Tulk, B. M., Townsend, R. R., and Verkman, A. S. (1998) Expression and characterization of the NBD1-R domain region of CFTR: Evidence for subunit-subunit interactions. Biochemistry 37, 2401-2409.
    • (1998) Biochemistry , vol.37 , pp. 2401-2409
    • Neville, D.C.1    Rozanas, C.R.2    Tulk, B.M.3    Townsend, R.R.4    Verkman, A.S.5
  • 3
    • 0030860084 scopus 로고    scopus 로고
    • The cystic fibrosis transmembrane conductance regulator and ATP
    • Devidas, S., and Guggino, W. B. (1997) The cystic fibrosis transmembrane conductance regulator and ATP. [Review] [53 refs]. Curr. Opin. Cell Biol. 9, 547-552.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 547-552
    • Devidas, S.1    Guggino, W.B.2
  • 4
    • 0030033151 scopus 로고    scopus 로고
    • A recombinant peptide model of the first nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator: Comparison of wild-type and delta F508 mutant forms
    • Yike, I., Ye, J., Zhang, Y., Manavalan, P., Gerken, T. A., and Dearborn, D. G. (1996) A recombinant peptide model of the first nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator: Comparison of wild-type and delta F508 mutant forms. Protein Sci. 5, 89-97.
    • (1996) Protein Sci. , vol.5 , pp. 89-97
    • Yike, I.1    Ye, J.2    Zhang, Y.3    Manavalan, P.4    Gerken, T.A.5    Dearborn, D.G.6
  • 6
    • 0026580010 scopus 로고
    • Intrinsic anion channel activity of the recombinant first nucleotide binding fold domain of the cystic fibrosis transmembrane regulator protein
    • Arispe, N., Rojas, E., Hartman, J., Sorscher, E. J., and Pollard, H. B. (1992) Intrinsic anion channel activity of the recombinant first nucleotide binding fold domain of the cystic fibrosis transmembrane regulator protein. Proc. Natl. Acad. Sci. USA 89, 1539-1543.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1539-1543
    • Arispe, N.1    Rojas, E.2    Hartman, J.3    Sorscher, E.J.4    Pollard, H.B.5
  • 7
    • 0026702994 scopus 로고
    • Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product
    • Hartman, J., Huang, Z., Rado, T. A., Peng, S., Jilling, T., Muccio, D. D., and Sorscher, E. J. (1992) Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product. J. Biol. Chem. 267, 6455-6458.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6455-6458
    • Hartman, J.1    Huang, Z.2    Rado, T.A.3    Peng, S.4    Jilling, T.5    Muccio, D.D.6    Sorscher, E.J.7
  • 8
    • 0029113976 scopus 로고
    • The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase
    • Ko, Y. H., and Pedersen, P. L. (1995). The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase. J. Biol. Chem. 270, 22093-22096.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22093-22096
    • Ko, Y.H.1    Pedersen, P.L.2
  • 9
    • 0032936619 scopus 로고    scopus 로고
    • Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis
    • Gadsby, D. C., and Nairn, A. C. (1999) Control of CFTR channel gating by phosphorylation and nucleotide hydrolysis. Physiol Rev. 79, S77-S106.
    • (1999) Physiol Rev. , vol.79
    • Gadsby, D.C.1    Nairn, A.C.2
  • 10
    • 6844258858 scopus 로고    scopus 로고
    • Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/reca topology: Structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Bianchet, M. A., Ko, Y. H., Amzel, L. M., and Pedersen, P. L. (1997) Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/recA topology: Structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR). J. Bioenerg. Biomembr. 29, 503-524.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 503-524
    • Bianchet, M.A.1    Ko, Y.H.2    Amzel, L.M.3    Pedersen, P.L.4
  • 11
    • 0028051797 scopus 로고
    • PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signal-regulated ATPase activity
    • Delepelaire, P. (1994) PrtD, the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system, exhibits a secretion signal-regulated ATPase activity. J. Biol. Cheistry. 269, 27952-27957.
    • (1994) J. Biol. Cheistry. , vol.269 , pp. 27952-27957
    • Delepelaire, P.1
  • 12
    • 0027190678 scopus 로고
    • ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator H1yB
    • Koronakis, V., Hughes, C., and Koronakis, E. (1993) ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator H1yB. Mol. Microbiol. 8, 1163-1175.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1163-1175
    • Koronakis, V.1    Hughes, C.2    Koronakis, E.3
  • 13
    • 0029883258 scopus 로고    scopus 로고
    • Lack of conventional ATPase properties in CFTR chloride channel gating
    • Schultz, B. D., Bridges, R. J., and Frizzell, R. A. (1996) Lack of conventional ATPase properties in CFTR chloride channel gating. J. Membr. Biol. 151, 63-75.
    • (1996) J. Membr. Biol. , vol.151 , pp. 63-75
    • Schultz, B.D.1    Bridges, R.J.2    Frizzell, R.A.3
  • 14
    • 0028340159 scopus 로고
    • Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis
    • Hwang, T. C., Nagel, G., Nairn, A. C., and Gadsby, D. C. (1994) Regulation of the gating of cystic fibrosis transmembrane conductance regulator Cl channels by phosphorylation and ATP hydrolysis. Proc. Natl. Acad. Sci. USA 91, 4698-4702.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4698-4702
    • Hwang, T.C.1    Nagel, G.2    Nairn, A.C.3    Gadsby, D.C.4
  • 15
    • 0027938084 scopus 로고
    • Regulation of CFTR channel gating
    • Gadsby, D. C., and Nairn, A. C. (1994) Regulation of CFTR channel gating. Trends Biochem. Sci. 19, 513-518.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 513-518
    • Gadsby, D.C.1    Nairn, A.C.2
  • 18
    • 0025912486 scopus 로고
    • Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide-binding domains 1 and 2
    • Gregory, R. J., Rich, D. P., Cheng, S. H., Souza, D. W., Paul, S., Manavalan, P., Anderson, M. P., Welsh, M. J., and Smith, A. E. (1991) Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide-binding domains 1 and 2. Mol. Cell. Biol. 11, 3886-3893.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3886-3893
    • Gregory, R.J.1    Rich, D.P.2    Cheng, S.H.3    Souza, D.W.4    Paul, S.5    Manavalan, P.6    Anderson, M.P.7    Welsh, M.J.8    Smith, A.E.9
  • 19
    • 0027162649 scopus 로고
    • Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis
    • Welsh, M. J., and Smith, A. E. (1993) Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. [Review] [26 refs]. Cell 73, 1251-1254.
    • (1993) Cell , vol.73 , pp. 1251-1254
    • Welsh, M.J.1    Smith, A.E.2
  • 20
    • 0026168359 scopus 로고
    • Probing the basic defect in cystic fibrosis
    • Tsui, L. C. (1991) Probing the basic defect in cystic fibrosis. [Review] [39 refs]. Curr. Opin. Genet. Dev. 1, 4-10.
    • (1991) Curr. Opin. Genet. Dev. , vol.1 , pp. 4-10
    • Tsui, L.C.1
  • 21
    • 0026667894 scopus 로고
    • Regulation by ATP and ADP of CFTR chloride channels that contain mutant nucleotide-binding domains
    • published erratum appears in Science (1992) 258(5089), 1719
    • Anderson, M. P., and Welsh, M. J. (1992) Regulation by ATP and ADP of CFTR chloride channels that contain mutant nucleotide-binding domains [published erratum appears in Science (1992) 258(5089), 1719]. Science 257, 1701-1704.
    • (1992) Science , vol.257 , pp. 1701-1704
    • Anderson, M.P.1    Welsh, M.J.2
  • 23
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones, P. M., and George, A. M. (1999) Subunit interactions in ABC transporters: Towards a functional architecture [in press citation]. FEMS Microbiol. Lett. 179, 187-202.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 24
    • 0021424434 scopus 로고
    • Organic extraction of Pi with isobutanol/ toluene
    • Shacter, E. (1984) Organic extraction of Pi with isobutanol/ toluene. Anal. Biochem. 138, 416-420.
    • (1984) Anal. Biochem. , vol.138 , pp. 416-420
    • Shacter, E.1
  • 25
    • 0006868693 scopus 로고
    • Organic extraction of inorganic phosphate
    • Nelson, N. (1980) Organic extraction of inorganic phosphate. Methods Enzymol. 69, 301-313.
    • (1980) Methods Enzymol. , vol.69 , pp. 301-313
    • Nelson, N.1
  • 26
    • 0033562963 scopus 로고    scopus 로고
    • Inhibition of ATPase, GTPase and adenylate kinase activities of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator by genistein
    • Randak, C., Auerswald, E. A., Assfalg-Machleidt, I., Reenstra, W. W., and Machleidt, W. (1999) Inhibition of ATPase, GTPase and adenylate kinase activities of the second nucleotide-binding fold of the cystic fibrosis transmembrane conductance regulator by genistein. Biochem, J. 340, 227-235.
    • (1999) Biochem, J. , vol.340 , pp. 227-235
    • Randak, C.1    Auerswald, E.A.2    Assfalg-Machleidt, I.3    Reenstra, W.W.4    Machleidt, W.5
  • 29
    • 0030773897 scopus 로고    scopus 로고
    • Genistein potentiates wild-type and delta F508-CFTR channel activity
    • Hwang, T. C., Wang, F., Yang, I. C., and Reenstra, W. W. (1997) Genistein potentiates wild-type and delta F508-CFTR channel activity. Am. J. Physiol. 273, C988-998.
    • (1997) Am. J. Physiol. , vol.273
    • Hwang, T.C.1    Wang, F.2    Yang, I.C.3    Reenstra, W.W.4
  • 30
    • 0031045778 scopus 로고    scopus 로고
    • Functional expression and apical localization of the cystic fibrosis transmembrane conductance regulator in MDCK I cells
    • Mohamed, A., Ferguson, D., Seibert, F. S., Cai, H. M., Kartner, N., Grinstein, S., Riordan, J. R., and Lukacs, G. L. (1997) Functional expression and apical localization of the cystic fibrosis transmembrane conductance regulator in MDCK I cells. Biochem. J. 322, 259-265.
    • (1997) Biochem. J. , vol.322 , pp. 259-265
    • Mohamed, A.1    Ferguson, D.2    Seibert, F.S.3    Cai, H.M.4    Kartner, N.5    Grinstein, S.6    Riordan, J.R.7    Lukacs, G.L.8
  • 31
    • 0030994053 scopus 로고    scopus 로고
    • Properties of chloride-conductive pathways in rat kidney cortical and outer-medulla brush-border membranes - Inhibition by anti-(cystic fibrosis transmembrane regulator) mAbs
    • Benharouga, M., Fritsch, J., Banting, G., and Edelman, A. (1997) Properties of chloride-conductive pathways in rat kidney cortical and outer-medulla brush-border membranes - Inhibition by anti-(cystic fibrosis transmembrane regulator) mAbs. Eur. J. Biochem. 246, 367-372.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 367-372
    • Benharouga, M.1    Fritsch, J.2    Banting, G.3    Edelman, A.4
  • 33
    • 0025921830 scopus 로고
    • Stimulation of secretion by the T84 colonic epithelial cell line with dietary flavonols
    • Nguyen, T. D., Canada, A. T., Heintz, G. G., Gettys, T. W., and Cohn, J. A. (1991) Stimulation of secretion by the T84 colonic epithelial cell line with dietary flavonols. Biochem. Pharmacol. 41, 1879-1886.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1879-1886
    • Nguyen, T.D.1    Canada, A.T.2    Heintz, G.G.3    Gettys, T.W.4    Cohn, J.A.5
  • 34
    • 0024278891 scopus 로고
    • Characterization of a protein serine kinase from yeast plasma membrane
    • Kolarov, J., Kulpa, J., Baijot, M., and Goffeau, A. (1988) Characterization of a protein serine kinase from yeast plasma membrane. J. Biol. Chem.. 263, 10613-10619.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10613-10619
    • Kolarov, J.1    Kulpa, J.2    Baijot, M.3    Goffeau, A.4
  • 35
    • 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
  • 36
    • 0027523995 scopus 로고
    • Regulation of membrane chloride currents in rat bile duct epithelial cells
    • Fitz, J. G., Basavappa, S., McGill, J., Melhus, O., and Cohn, J. A. (1993) Regulation of membrane chloride currents in rat bile duct epithelial cells. J. Clin. Invest. 91, 319-328.
    • (1993) J. Clin. Invest. , vol.91 , pp. 319-328
    • Fitz, J.G.1    Basavappa, S.2    McGill, J.3    Melhus, O.4    Cohn, J.A.5
  • 37
    • 0033027269 scopus 로고    scopus 로고
    • Activation of wild-type and deltaF508-CFTR by phosphodiesterase inhibitors through cAMP-dependent and -independent mechanisms
    • al-Nakkash, L., and Hwang, T. C. (1999) Activation of wild-type and deltaF508-CFTR by phosphodiesterase inhibitors through cAMP-dependent and -independent mechanisms. Pflugers Arch. Eur. J. Physiol. 437, 553-561.
    • (1999) Pflugers Arch. Eur. J. Physiol. , vol.437 , pp. 553-561
    • Al-Nakkash, L.1    Hwang, T.C.2
  • 40
    • 0342517347 scopus 로고
    • CPX control of calcium-dependent aggregation of biological membranes and acidic phospholipid liposomes driven by nucleotide binding fold-1 (NBF1) domain from CFTR
    • Lee, G., Huang, Z., Wang, Y., Sorscher, E., Jacobson, K. A., Barnoy, S., and Pollard, H. B. (1995) CPX control of calcium-dependent aggregation of biological membranes and acidic phospholipid liposomes driven by nucleotide binding fold-1 (NBF1) domain from CFTR. Pediatr. Pulmonol. S12, 185-185.
    • (1995) Pediatr. Pulmonol. , vol.S12 , pp. 185-185
    • Lee, G.1    Huang, Z.2    Wang, Y.3    Sorscher, E.4    Jacobson, K.A.5    Barnoy, S.6    Pollard, H.B.7
  • 41
    • 0343324308 scopus 로고    scopus 로고
    • CPX binds to 30 residue peptide domain I-alpha (CFTR[477-508]) from first nucleotide binding fold, and potentiates peptide-membrane interactions
    • Lee, G., Cohen, B. E., Barnoy, S., Eidelman, O., Jacobson, K. A., and Pollard, H. B. (1998) CPX binds to 30 residue peptide domain I-alpha (CFTR[477-508]) from first nucleotide binding fold, and potentiates peptide-membrane interactions. Pediatr. Pulmonol. Suppl. S12, 185-185.
    • (1998) Pediatr. Pulmonol. Suppl. , vol.S12 , pp. 185-185
    • Lee, G.1    Cohen, B.E.2    Barnoy, S.3    Eidelman, O.4    Jacobson, K.A.5    Pollard, H.B.6
  • 45
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L-W., Wang, I. X., Nikaido, K., Liu, P-Q., Ames, G. F., and Kim, S-H. (1998) Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396, 703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.-W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.-Q.4    Ames, G.F.5    Kim, S.-H.6
  • 46
    • 0010113752 scopus 로고    scopus 로고
    • Frontiers in research on cystic fibrosis: Understanding its molecular and chemical basis and relationship to the pathogenesis of the disease
    • Ko, Y. H., and Pedersen, P. L. (1997) Frontiers in research on cystic fibrosis: understanding its molecular and chemical basis and relationship to the pathogenesis of the disease. [Review] [101 refs]. J. Bioenerg. Biomembr. 29, 417-427.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 417-427
    • Ko, Y.H.1    Pedersen, P.L.2
  • 47
    • 0028362501 scopus 로고
    • Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein
    • Urbatsch, I. L., al-Shawi, M. K., and Senior, A. E. (1994) Characterization of the ATPase activity of purified Chinese hamster P-glycoprotein. Biochemistry 33, 7069-7076.
    • (1994) Biochemistry , vol.33 , pp. 7069-7076
    • Urbatsch, I.L.1    Al-Shawi, M.K.2    Senior, A.E.3
  • 49
    • 0039550861 scopus 로고    scopus 로고
    • Nucleotide occlusion in the human cystic fibrosis transmembrane conductance regulator. Different patterns in the two nucleotide binding domains
    • Szabo, K., Szakacs, G., Hegeds, T., and Sarkadi, B. (1999) Nucleotide occlusion in the human cystic fibrosis transmembrane conductance regulator. Different patterns in the two nucleotide binding domains. J. Biol. Chem. 274, 12209-12212.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12209-12212
    • Szabo, K.1    Szakacs, G.2    Hegeds, T.3    Sarkadi, B.4
  • 50
    • 0030943895 scopus 로고    scopus 로고
    • 8-Cyclopentyl-1,3-dipropylxanthine and other xanthines differentially bind to the wild-type and delta F508 first nucleotide binding fold (NBF-1) domains of the cystic fibrosis transmembrane conductance regulator
    • Cohen, B. E., Lee, G., Jacobson, K. A., Kim, Y. C., Huang, Z., Sorscher, E. J., and Pollard, H. B. (1997) 8-Cyclopentyl-1,3-dipropylxanthine and other xanthines differentially bind to the wild-type and delta F508 first nucleotide binding fold (NBF-1) domains of the cystic fibrosis transmembrane conductance regulator. Biochemistry 36, 6455-6461.
    • (1997) Biochemistry , vol.36 , pp. 6455-6461
    • Cohen, B.E.1    Lee, G.2    Jacobson, K.A.3    Kim, Y.C.4    Huang, Z.5    Sorscher, E.J.6    Pollard, H.B.7
  • 51
    • 0026472873 scopus 로고
    • Traffic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames, G. F., Mimura, C., Holbrook, S., and Shyamala, V. (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.1    Mimura, C.2    Holbrook, S.3    Shyamala, V.4
  • 52
    • 0027364318 scopus 로고
    • Functional roles of the nucleotide-binding folds in the activation of the cystic fibrosis transmembrane conductance regulator
    • Smit, L. S., Wilkinson, D. J., Mansoura, M. K., Collins, F. S., and Dawson, D. C. (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


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