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Volumn 144, Issue 4, 2014, Pages 321-336

Structure-activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects

Author keywords

[No Author keywords available]

Indexed keywords

5-NITRO-2-(3-PHENYLPROPYLAMINO)BENZOIC ACID; ADENOSINE TRIPHOSPHATE; CHLORIDE CHANNEL; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; NITROBENZOIC ACID DERIVATIVE;

EID: 84908227848     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201411246     Document Type: Article
Times cited : (11)

References (36)
  • 1
    • 73149086415 scopus 로고    scopus 로고
    • An electrostatic interaction between TEA and an introduced pore aromatic drives spring-in-the-door inactivation in Shaker potassium channels
    • Ahern, C.A., A.L. Eastwood, D.A. Dougherty, and R. Horn. 2009. An electrostatic interaction between TEA and an introduced pore aromatic drives spring-in-the-door inactivation in Shaker potassium channels. J. Gen. Physiol. 134:461-469. http://dx.doi.org/10 .1085/jgp.200910260
    • (2009) J. Gen. Physiol. , vol.134 , pp. 461-469
    • Ahern, C.A.1    Eastwood, A.L.2    Dougherty, D.A.3    Horn, R.4
  • 2
    • 84856305229 scopus 로고    scopus 로고
    • Catalytic and transport cycles of ABC exporters
    • Al-Shawi, M.K. 2011. Catalytic and transport cycles of ABC exporters. Essays Biochem. 50:63-83. http://dx.doi.org/10.1042/bse0500063
    • (2011) Essays Biochem. , vol.50 , pp. 63-83
    • Al-Shawi, M.K.1
  • 3
    • 0037013262 scopus 로고    scopus 로고
    • The first nucleotide binding domain of cystic fibrosis transmembrane conductance regulator is a site of stable nucleotide interaction, whereas the second is a site of rapid turnover
    • Aleksandrov, L., A.A. Aleksandrov, X.B. Chang, and J.R. Riordan. 2002. The first nucleotide binding domain of cystic fibrosis transmembrane conductance regulator is a site of stable nucleotide interaction, whereas the second is a site of rapid turnover. J. Biol. Chem. 277:15419-15425. http://dx.doi.org/10.1074/jbc.M111713200
    • (2002) J. Biol. Chem. , vol.277 , pp. 15419-15425
    • Aleksandrov, L.1    Aleksandrov, A.A.2    Chang, X.B.3    Riordan, J.R.4
  • 4
    • 0141513675 scopus 로고    scopus 로고
    • Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating
    • Basso, C., P. Vergani, A.C. Nairn, and D.C. Gadsby. 2003. Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating. J. Gen. Physiol. 122:333-348. http://dx.doi.org/10.1085/jgp.200308798
    • (2003) J. Gen. Physiol. , vol.122 , pp. 333-348
    • Basso, C.1    Vergani, P.2    Nairn, A.C.3    Gadsby, D.C.4
  • 5
    • 84904002908 scopus 로고    scopus 로고
    • A CFTR corrector (lumacaftor) and a CFTR potentiator (ivacaftor) for treatment of patients with cystic fibrosis who have a phe508del CFTR mutation: a phase 2 randomised controlled trial
    • Boyle, M.P., S.C. Bell, M.W. Konstan, S.A. McColley, S.M. Rowe, E. Rietschel, X. Huang, D. Waltz, N.R. Patel, and D. Rodman; VX09- 809-102 Study Group. 2014. A CFTR corrector (lumacaftor) and a CFTR potentiator (ivacaftor) for treatment of patients with cystic fibrosis who have a phe508del CFTR mutation: a phase 2 randomised controlled trial. Lancet Respir. Med. 2:527-538. http:// dx.doi.org/10.1016/S2213-2600(14)70132-8
    • (2014) Lancet Respir. Med. , vol.2 , pp. 527-538
    • Boyle, M.P.1    Bell, S.C.2    Konstan, M.W.3    McColley, S.A.4    Rowe, S.M.5    Rietschel, E.6    Huang, X.7    Waltz, D.8    Patel, N.R.9    Rodman, D.10
  • 6
    • 0033886092 scopus 로고    scopus 로고
    • Severed molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH2- terminal nucleotide binding domain
    • Chan, K.W., L. Csanády, D. Seto-Young, A.C. Nairn, and D.C. Gadsby. 2000. Severed molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH2- terminal nucleotide binding domain. J. Gen. Physiol. 116:163-180. http://dx.doi.org/10.1085/jgp.116.2.163
    • (2000) J. Gen. Physiol. , vol.116 , pp. 163-180
    • Chan, K.W.1    Csanády, L.2    Seto-Young, D.3    Nairn, A.C.4    Gadsby, D.C.5
  • 7
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng, S.H., R.J. Gregory, J. Marshall, S. Paul, D.W. Souza, G.A. White, C.R. O'Riordan, and A.E. Smith. 1990. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell. 63:827-834. http://dx.doi.org/10 .1016/0092-8674(90)90148-8
    • (1990) Cell. , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6    O'Riordan, C.R.7    Smith, A.E.8
  • 9
    • 17144456826 scopus 로고    scopus 로고
    • Rapid kinetic analysis of multichannel records by a simultaneous fit to all dwell-time histograms
    • Csanády, L. 2000. Rapid kinetic analysis of multichannel records by a simultaneous fit to all dwell-time histograms. Biophys. J. 78:785- 799. http://dx.doi.org/10.1016/S0006-3495(00)76636-7
    • (2000) Biophys. J. , vol.78 , pp. 785- 799
    • Csanády, L.1
  • 10
    • 84893069291 scopus 로고    scopus 로고
    • Catalyst-like modulation of transition states for CFTR channel opening and closing: new stimulation strategy exploits nonequilibrium gating
    • Csanády, L., and B. Töröcsik. 2014. Catalyst-like modulation of transition states for CFTR channel opening and closing: new stimulation strategy exploits nonequilibrium gating. J. Gen. Physiol. 143:269-287. http://dx.doi.org/10.1085/jgp.201311089
    • (2014) J. Gen. Physiol. , vol.143 , pp. 269-287
    • Csanády, L.1    Töröcsik, B.2
  • 11
    • 0033817333 scopus 로고    scopus 로고
    • Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains
    • Csanády, L., K.W. Chan, D. Seto-Young, D.C. Kopsco, A.C. Nairn, and D.C. Gadsby. 2000. Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains. J. Gen. Physiol. 116:477-500. http://dx.doi.org/ 10.1085/jgp.116.3.477
    • (2000) J. Gen. Physiol. , vol.116 , pp. 477-500
    • Csanády, L.1    Chan, K.W.2    Seto-Young, D.3    Kopsco, D.C.4    Nairn, A.C.5    Gadsby, D.C.6
  • 12
    • 33750499982 scopus 로고    scopus 로고
    • Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle
    • Csanády, L., A.C. Nairn, and D.C. Gadsby. 2006. Thermodynamics of CFTR channel gating: a spreading conformational change initiates an irreversible gating cycle. J. Gen. Physiol. 128:523-533. http://dx.doi.org/10.1085/jgp.200609558
    • (2006) J. Gen. Physiol. , vol.128 , pp. 523-533
    • Csanády, L.1    Nairn, A.C.2    Gadsby, D.C.3
  • 13
    • 75749153312 scopus 로고    scopus 로고
    • - ion pore revealed by distributions of open channel burst durations
    • - ion pore revealed by distributions of open channel burst durations. Proc. Natl. Acad. Sci. USA. 107:1241-1246. http://dx.doi.org/10.1073/pnas .0911061107
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 1241-1246
    • Csanády, L.1    Vergani, P.2    Gadsby, D.C.3
  • 14
    • 84864258150 scopus 로고    scopus 로고
    • New model of cystic fibrosis transmembrane conductance regulator proposes active channel-like conformation
    • Dalton, J., O. Kalid, M. Schushan, N. Ben-Tal, and J. Villà-Freixa. 2012. New model of cystic fibrosis transmembrane conductance regulator proposes active channel-like conformation. J. Chem. Inf. Model. 52:1842-1853. http://dx.doi.org/10.1021/ci2005884
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 1842-1853
    • Dalton, J.1    Kalid, O.2    Schushan, M.3    Ben-Tal, N.4    Villà-Freixa, J.5
  • 15
    • 25844487733 scopus 로고    scopus 로고
    • Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates
    • Dean, M., and T. Annilo. 2005. Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. Annu. Rev. Genomics Hum. Genet. 6:123-142. http://dx.doi.org/10.1146/annurev.genom .6.080604.162122
    • (2005) Annu. Rev. Genomics Hum. Genet. , vol.6 , pp. 123-142
    • Dean, M.1    Annilo, T.2
  • 16
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby, D.C., P. Vergani, and L. Csanády. 2006. The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature. 440:477-483. http://dx.doi.org/10.1038/nature04712
    • (2006) Nature. , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanády, L.3
  • 17
    • 0029117303 scopus 로고
    • Conformational states of CFTR associated with channel gating: the role ATP binding and hydrolysis
    • Gunderson, K.L., and R.R. Kopito. 1995. Conformational states of CFTR associated with channel gating: the role ATP binding and hydrolysis. Cell. 82:231-239. http://dx.doi.org/10.1016/0092- 8674(95)90310-0
    • (1995) Cell. , vol.82 , pp. 231-239
    • Gunderson, K.L.1    Kopito, R.R.2
  • 18
    • 34548853133 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporter proteins
    • Hollenstein, K., R.J. Dawson, and K.P. Locher. 2007. Structure and mechanism of ABC transporter proteins. Curr. Opin. Struct. Biol. 17:412-418. http://dx.doi.org/10.1016/j.sbi.2007.07.003
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 412-418
    • Hollenstein, K.1    Dawson, R.J.2    Locher, K.P.3
  • 19
    • 65749102092 scopus 로고    scopus 로고
    • - channel by ATP-driven nucleotide-binding domain dimerisation
    • - channel by ATP-driven nucleotide-binding domain dimerisation. J. Physiol. 587:2151-2161. http://dx.doi.org/10.1113/jphysiol.2009 .171595
    • (2009) J. Physiol. , vol.587 , pp. 2151-2161
    • Hwang, T.C.1    Sheppard, D.N.2
  • 20
    • 84875048537 scopus 로고    scopus 로고
    • Vx-770 potentiates CFTR function by promoting decoupling between the gating cycle and ATP hydrolysis cycle
    • Jih, K.Y., and T.C. Hwang. 2013. Vx-770 potentiates CFTR function by promoting decoupling between the gating cycle and ATP hydrolysis cycle. Proc. Natl. Acad. Sci. USA. 110:4404-4409. http:// dx.doi.org/10.1073/pnas.1215982110
    • (2013) Proc. Natl. Acad. Sci. USA. , vol.110 , pp. 4404-4409
    • Jih, K.Y.1    Hwang, T.C.2
  • 21
    • 84870795585 scopus 로고    scopus 로고
    • Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation
    • Jih, K.Y., Y. Sohma, and T.C. Hwang. 2012. Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation. J. Gen. Physiol. 140:347-359. http://dx.doi.org/10.1085/jgp.201210834
    • (2012) J. Gen. Physiol. , vol.140 , pp. 347-359
    • Jih, K.Y.1    Sohma, Y.2    Hwang, T.C.3
  • 22
    • 84926090443 scopus 로고    scopus 로고
    • Combined effects of VX-770 and VX-809 on several functional abnormalities of F508del-CFTR channels
    • Kopeikin, Z., Z. Yuksek, H.Y. Yang, and S.G. Bompadre. 2014. Combined effects of VX-770 and VX-809 on several functional abnormalities of F508del-CFTR channels. J. Cyst. Fibros. http:// dx.doi.org/10.1016/j.jcf.2014.04.003
    • (2014) J. Cyst. Fibros
    • Kopeikin, Z.1    Yuksek, Z.2    Yang, H.Y.3    Bompadre, S.G.4
  • 23
    • 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. http://dx.doi.org/10.1074/jbc.M414354200
    • (2005) J. Biol. Chem. , vol.280 , pp. 8945-8950
    • Linsdell, P.1
  • 24
    • 0030886246 scopus 로고    scopus 로고
    • Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell, P., J.A. Tabcharani, and J.W. Hanrahan. 1997. Multi-ion mechanism for ion permeation and block in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 110:365-377. http://dx.doi.org/10.1085/jgp.110.4.365
    • (1997) J. Gen. Physiol. , vol.110 , pp. 365-377
    • Linsdell, P.1    Tabcharani, J.A.2    Hanrahan, J.W.3
  • 25
    • 77953796491 scopus 로고    scopus 로고
    • Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs
    • Miki, H., Z. Zhou, M. Li, T.C. Hwang, and S.G. Bompadre. 2010. Potentiation of disease-associated cystic fibrosis transmembrane conductance regulator mutants by hydrolyzable ATP analogs. J. Biol. Chem. 285:19967-19975. http://dx.doi.org/10.1074/ jbc.M109.092684
    • (2010) J. Biol. Chem. , vol.285 , pp. 19967-19975
    • Miki, H.1    Zhou, Z.2    Li, M.3    Hwang, T.C.4    Bompadre, S.G.5
  • 26
    • 0033514315 scopus 로고    scopus 로고
    • Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator)
    • Ramjeesingh, M., C. Li, E. Garami, L.J. Huan, K. Galley, Y. Wang, and C.E. Bear. 1999. Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator). Biochemistry. 38:1463-1468. http://dx.doi.org/10.1021/bi982243y
    • (1999) Biochemistry. , vol.38 , pp. 1463-1468
    • Ramjeesingh, M.1    Li, C.2    Garami, E.3    Huan, L.J.4    Galley, K.5    Wang, Y.6    Bear, C.E.7
  • 29
    • 77951706563 scopus 로고    scopus 로고
    • Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel
    • Tsai, M.F., M. Li, and T.C. Hwang. 2010. Stable ATP binding mediated by a partial NBD dimer of the CFTR chloride channel. J. Gen. Physiol. 135:399-414. http://dx.doi.org/10.1085/jgp.201010399
    • (2010) J. Gen. Physiol. , vol.135 , pp. 399-414
    • Tsai, M.F.1    Li, M.2    Hwang, T.C.3
  • 34
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide- binding domains
    • Vergani, P., S.W. Lockless, A.C. Nairn, and D.C. Gadsby. 2005. CFTR channel opening by ATP-driven tight dimerization of its nucleotide- binding domains. Nature. 433:876-880. http://dx.doi.org/ 10.1038/nature03313
    • (2005) Nature. , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 35
    • 21244494942 scopus 로고    scopus 로고
    • Activating cystic fibrosis transmembrane conductance regulator channels with pore blocker analogs
    • Wang, W., G. Li, J.P. Clancy, and K.L. Kirk. 2005. Activating cystic fibrosis transmembrane conductance regulator channels with pore blocker analogs. J. Biol. Chem. 280:23622-23630. http://dx.doi .org/10.1074/jbc.M503118200
    • (2005) J. Biol. Chem. , vol.280 , pp. 23622-23630
    • Wang, W.1    Li, G.2    Clancy, J.P.3    Kirk, K.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.