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Volumn 139, Issue 5, 2012, Pages 359-370

Identification of a novel post-hydrolytic state in CFTR gating

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; DIPHOSPHORIC ACID; PYROPHOSPHATE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 84861167188     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210789     Document Type: Article
Times cited : (19)

References (42)
  • 2
    • 77956237499 scopus 로고    scopus 로고
    • Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation
    • Bai, Y., M. Li, and T.C. Hwang. 2010. Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation. J. Gen. Physiol. 136:293-309. http://dx.doi.org/10.1085/jgp.201010480
    • (2010) J. Gen. Physiol. , vol.136 , pp. 293-309
    • Bai, Y.1    Li, M.2    Hwang, T.C.3
  • 3
    • 80555127440 scopus 로고    scopus 로고
    • Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7)
    • Bai, Y., M. Li, and T.C. Hwang. 2011. Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7). J. Gen. Physiol. 138:495-507. http://dx.doi.org/10.1085/jgp.201110705
    • (2011) J. Gen. Physiol. , vol.138 , pp. 495-507
    • Bai, Y.1    Li, M.2    Hwang, T.C.3
  • 4
    • 0026532895 scopus 로고
    • Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Bear, C.E., C.H. Li, N. Kartner, R.J. Bridges, T.J. Jensen, M. Ramjeesingh, and J.R. Riordan. 1992. Purification and functional reconstitution of the cystic fibrosis transmembrane conductance regulator (CFTR). Cell. 68:809-818. http://dx.doi.org/10.1016/0092-8674(92)90155-6
    • (1992) Cell , vol.68 , pp. 809-818
    • Bear, C.E.1    Li, C.H.2    Kartner, N.3    Bridges, R.J.4    Jensen, T.J.5    Ramjeesingh, M.6    Riordan, J.R.7
  • 5
    • 17044383747 scopus 로고    scopus 로고
    • CFTR gating I: Characterization of the ATPdependent gating of a phosphorylation-independent CFTR channel (ΔR-CFTR)
    • Bompadre, S.G., T. Ai, J.H. Cho, X. Wang, Y. Sohma, M. Li, and T.C. Hwang. 2005a. CFTR gating I: Characterization of the ATPdependent gating of a phosphorylation-independent CFTR channel (ΔR-CFTR). J. Gen. Physiol. 125:361-375. http://dx.doi.org/10.1085/jgp.200409227
    • (2005) J. Gen. Physiol. , vol.125 , pp. 361-375
    • Bompadre, S.G.1    Ai, T.2    Cho, J.H.3    Wang, X.4    Sohma, Y.5    Li, M.6    Hwang, T.C.7
  • 6
    • 17044401724 scopus 로고    scopus 로고
    • CFTR gating II: Effects of nucleotide binding on the stability of open states
    • Bompadre, S.G., J.H. Cho, X. Wang, X. Zou, Y. Sohma, M. Li, and T.C. Hwang. 2005b. CFTR gating II: Effects of nucleotide binding on the stability of open states. J. Gen. Physiol. 125:377-394. http://dx.doi.org/10.1085/jgp.200409228
    • (2005) J. Gen. Physiol. , vol.125 , pp. 377-394
    • Bompadre, S.G.1    Cho, J.H.2    Wang, X.3    Zou, X.4    Sohma, Y.5    Li, M.6    Hwang, T.C.7
  • 7
    • 33644863604 scopus 로고    scopus 로고
    • Differential sensitivity of the cystic fibrosis (CF)-associated mutants G551D and G1349D to potentiators of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel
    • Cai, Z., A. Taddei, and D.N. Sheppard. 2006. Differential sensitivity of the cystic fibrosis (CF)-associated mutants G551D and G1349D to potentiators of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel. J. Biol. Chem. 281:1970-1977. http://dx.doi.org/10.1074/jbc.M510576200
    • (2006) J. Biol. Chem. , vol.281 , pp. 1970-1977
    • Cai, Z.1    Taddei, A.2    Sheppard, D.N.3
  • 8
    • 0028906612 scopus 로고
    • The two nucleotidebinding 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 nucleotidebinding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity. J. Biol. Chem. 270:1711-1717. http://dx.doi.org/10.1074/jbc.270.4.1711
    • (1995) J. Biol. Chem. , vol.270 , pp. 1711-1717
    • Carson, M.R.1    Travis, S.M.2    Welsh, M.J.3
  • 9
    • 11844258265 scopus 로고    scopus 로고
    • A speed limit for conformational change of an allosteric membrane protein
    • Chakrapani, S., and A. Auerbach. 2005. A speed limit for conformational change of an allosteric membrane protein. Proc. Natl. Acad. Sci. USA. 102:87-92. http://dx.doi.org/10.1073/pnas.0406777102
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 87-92
    • Chakrapani, S.1    Auerbach, A.2
  • 10
    • 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
  • 11
    • 77951715890 scopus 로고    scopus 로고
    • Degenerate ABC composite site is stably glued together by trapped ATP
    • Csanády, L. 2010. Degenerate ABC composite site is stably glued together by trapped ATP. J. Gen. Physiol. 135:395-398. http://dx.doi.org/10.1085/jgp.201010443
    • (2010) J. Gen. Physiol. , vol.135 , pp. 395-398
    • Csanády, L.1
  • 12
    • 0033063094 scopus 로고    scopus 로고
    • CFTR channel gating: Incremental progress in irreversible steps
    • Csanády, L., and D.C. Gadsby. 1999. CFTR channel gating: Incremental progress in irreversible steps. J. Gen. Physiol. 114:49-53. http://dx.doi.org/10.1085/jgp.114.1.49
    • (1999) J. Gen. Physiol. , vol.114 , pp. 49-53
    • Csanády, L.1    Gadsby, D.C.2
  • 13
    • 12344263101 scopus 로고    scopus 로고
    • Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain
    • Csanády, L., K.W. Chan, A.C. Nairn, and D.C. Gadsby. 2005a. Functional roles of nonconserved structural segments in CFTR's NH2-terminal nucleotide binding domain. J. Gen. Physiol. 125:43-55. http://dx.doi.org/10.1085/jgp.200409174
    • (2005) J. Gen. Physiol. , vol.125 , pp. 3-55
    • Csanády, L.1    Chan, K.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 15
    • 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
  • 16
    • 75749153312 scopus 로고    scopus 로고
    • Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations
    • Csanády, L., P. Vergani, and D.C. Gadsby. 2010. Strict coupling between CFTR's catalytic cycle and gating of its Cl- 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
  • 17
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R.J., and K.P. Locher. 2006. Structure of a bacterial multidrug ABC transporter. Nature. 443:180-185. http://dx.doi.org/10.1038/nature05155
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 18
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R.J., and K.P. Locher. 2007. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 581:935-938. http://dx.doi.org/10.1016/j.febslet.2007.01.073
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 19
    • 0028070453 scopus 로고
    • Effects of pyrophosphate and nucleotide analogs suggest a role for ATP hydrolysis in cystic fibrosis transmembrane regulator channel gating
    • Gunderson, K.L., and R.R. Kopito. 1994. Effects of pyrophosphate and nucleotide analogs suggest a role for ATP hydrolysis in cystic fibrosis transmembrane regulator channel gating. J. Biol. Chem. 269:19349-19353.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19349-19353
    • Gunderson, K.L.1    Kopito, R.R.2
  • 20
    • 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
  • 21
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein, K., D.C. Frei, and K.P. Locher. 2007. Structure of an ABC transporter in complex with its binding protein. Nature. 446:213-216. http://dx.doi.org/10.1038/nature05626
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 22
    • 0028340159 scopus 로고
    • Regulation of the gating of cystic fibrosis transmembrane conductance regulator C1 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 C1 channels by phosphorylation and ATP hydrolysis. Proc. Natl. Acad. Sci. USA. 91:4698-4702. http://dx.doi.org/10.1073/pnas.91.11.4698
    • (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
  • 23
    • 33947284958 scopus 로고    scopus 로고
    • Dynamics and function in a bacterial ABC transporter: simulation studies of the BtuCDF system and its components
    • Ivetac, A., J.D. Campbell, and M.S. Sansom. 2007. Dynamics and function in a bacterial ABC transporter: simulation studies of the BtuCDF system and its components. Biochemistry. 46:2767-2778. http://dx.doi.org/10.1021/bi0622571
    • (2007) Biochemistry , vol.46 , pp. 2767-2778
    • Ivetac, A.1    Campbell, J.D.2    Sansom, M.S.3
  • 24
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare, D., M.L. Oldham, C. Orelle, A.L. Davidson, and J. Chen. 2009. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell. 33:528-536. http://dx.doi.org/10.1016/j.molcel.2009.01.035
    • (2009) Mol. Cell. , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 25
    • 78650045527 scopus 로고    scopus 로고
    • On the mechanism of CFTR inhibition by a thiazolidinone derivative
    • Kopeikin, Z., Y. Sohma, M. Li, and T.C. Hwang. 2010. On the mechanism of CFTR inhibition by a thiazolidinone derivative. J. Gen. Physiol. 136:659-671. http://dx.doi.org/10.1085/jgp.201010518
    • (2010) J. Gen. Physiol. , vol.136 , pp. 659-671
    • Kopeikin, Z.1    Sohma, Y.2    Li, M.3    Hwang, T.C.4
  • 27
    • 33750222000 scopus 로고    scopus 로고
    • In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer
    • Mense, M., P. Vergani, D.M. White, G. Altberg, A.C. Nairn, and D.C. Gadsby. 2006. In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer. EMBO J. 25:4728-4739. http://dx.doi.org/10.1038/sj.emboj.7601373
    • (2006) EMBO J , vol.25 , pp. 4728-4739
    • Mense, M.1    Vergani, P.2    White, D.M.3    Altberg, G.4    Nairn, A.C.5    Gadsby, D.C.6
  • 28
    • 0036521974 scopus 로고    scopus 로고
    • Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains
    • Powe, A.C., Jr., L. Al-Nakkash, M. Li, and T.C. Hwang. 2002. Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains. J. Physiol. 539:333-346. http://dx.doi.org/10.1113/jphysiol.2001.013162
    • (2002) J. Physiol. , vol.539 , pp. 333-346
    • Powe Jr., A.C.1    Al-Nakkash, L.2    Li, M.3    Hwang, T.C.4
  • 30
    • 79958076650 scopus 로고    scopus 로고
    • Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating
    • Szollosi, A., D.R. Muallem, L. Csanády, and P. Vergani. 2011. Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating. J. Gen. Physiol. 137:549-562. http://dx.doi.org/10.1085/jgp.201110608
    • (2011) J. Gen. Physiol. , vol.137 , pp. 549-562
    • Szollosi, A.1    Muallem, D.R.2    Csanády, L.3    Vergani, P.4
  • 31
    • 64549132504 scopus 로고    scopus 로고
    • Statedependent modulation of CFTR gating by pyrophosphate
    • Tsai, M.F., H. Shimizu, Y. Sohma, M. Li, and T.C. Hwang. 2009. Statedependent modulation of CFTR gating by pyrophosphate. J. Gen. Physiol. 133:405-419. http://dx.doi.org/10.1085/jgp.200810186
    • (2009) J. Gen. Physiol. , vol.133 , pp. 405-419
    • Tsai, M.F.1    Shimizu, H.2    Sohma, Y.3    Li, M.4    Hwang, T.C.5
  • 32
    • 78549242002 scopus 로고    scopus 로고
    • Optimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels
    • Tsai, M.F., K.Y. Jih, H. Shimizu, M. Li, and T.C. Hwang. 2010a. Optimization of the degenerated interfacial ATP binding site improves the function of disease-related mutant cystic fibrosis transmembrane conductance regulator (CFTR) channels. J. Biol. Chem. 285:37663-37671. http://dx.doi.org/10.1074/jbc.M110.172817
    • (2010) J. Biol. Chem. , vol.285 , pp. 37663-37671
    • Tsai, M.F.1    Jih, K.Y.2    Shimizu, H.3    Li, M.4    Hwang, T.C.5
  • 33
    • 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. 2010b. 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
  • 35
    • 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
  • 36
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward, A., C.L. Reyes, J. Yu, C.B. Roth, and G. Chang. 2007. Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc. Natl. Acad. Sci. USA. 104:19005-19010. http://dx.doi.org/10.1073/pnas.0709388104
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 37
    • 0028265949 scopus 로고
    • Effect of ATP concentration on CFTR Cl- channels: a kinetic analysis of channel regulation
    • Winter, M.C., D.N. Sheppard, M.R. Carson, and M.J. Welsh. 1994. Effect of ATP concentration on CFTR Cl- channels: a kinetic analysis of channel regulation. Biophys. J. 66:1398-1403. http://dx.doi.org/10.1016/S0006-3495(94)80930-0
    • (1994) Biophys. J. , vol.66 , pp. 1398-1403
    • Winter, M.C.1    Sheppard, D.N.2    Carson, M.R.3    Welsh, M.J.4
  • 39
    • 0032954806 scopus 로고    scopus 로고
    • Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis Quantitative analysis of a cyclic gating scheme
    • Zeltwanger, S., F. Wang, G.T. Wang, K.D. Gillis, and T.C. Hwang. 1999. Gating of cystic fibrosis transmembrane conductance regulator chloride channels by adenosine triphosphate hydrolysis. Quantitative analysis of a cyclic gating scheme. J. Gen. Physiol. 113:541-554. http://dx.doi.org/10.1085/jgp.113.4.541
    • (1999) J. Gen. Physiol. , vol.113 , pp. 541-554
    • Zeltwanger, S.1    Wang, F.2    Wang, G.T.3    Gillis, K.D.4    Hwang, T.C.5
  • 40
    • 0035870969 scopus 로고    scopus 로고
    • Voltage-dependent flickery block of an open cystic fibrosis transmembrane conductance regulator (CFTR) channel pore
    • Zhou, Z., S. Hu, and T.C. Hwang. 2001. Voltage-dependent flickery block of an open cystic fibrosis transmembrane conductance regulator (CFTR) channel pore. J. Physiol. 532:435-448. http://dx.doi.org/10.1111/j.1469-7793.2001.0435f.x
    • (2001) J. Physiol. , vol.532 , pp. 435-448
    • Zhou, Z.1    Hu, S.2    Hwang, T.C.3
  • 41
    • 29244490620 scopus 로고    scopus 로고
    • 2005 High affinity ATP/ADP analogues as new tools for studying CFTR gating
    • Zhou, Z., X. Wang, M. Li, Y. Sohma, X. Zou, and T.C. Hwang. 2005.High affinity ATP/ADP analogues as new tools for studying CFTR gating. J. Physiol. 569:447-457. http://dx.doi.org/10.1113/jphysiol.2005.095083
    • J. Physiol. , vol.569 , pp. 447-457
    • Zhou, Z.1    Wang, X.2    Li, M.3    Sohma, Y.4    Zou, X.5    Hwang, T.C.6
  • 42
    • 33749039521 scopus 로고    scopus 로고
    • The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics
    • Zhou, Z., X. Wang, H.Y. Liu, X. Zou, M. Li, and T.C. Hwang. 2006. The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics. J. Gen. Physiol. 128:413-422. http://dx.doi.org/10.1085/jgp.200609622
    • (2006) J. Gen. Physiol. , vol.128 , pp. 413-422
    • Zhou, Z.1    Wang, X.2    Liu, H.Y.3    Zou, X.4    Li, M.5    Hwang, T.C.6


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