메뉴 건너뛰기




Volumn 134, Issue 2, 2009, Pages 129-136

Application of rate-equilibrium free energy relationship analysis to nonequilibrium ion channel gating mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ION CHANNEL; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 67749084300     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.200910268     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 0032503962 scopus 로고    scopus 로고
    • Regulation of CFTR ion channel gating by MgATP
    • Aleksandrov, A.A., and J.R. Riordan. 1998. Regulation of CFTR ion channel gating by MgATP. FEBS Lett. 431:97-101.
    • (1998) FEBS Lett , vol.431 , pp. 97-101
    • Aleksandrov, A.A.1    Riordan, J.R.2
  • 2
    • 0033759953 scopus 로고    scopus 로고
    • The non-hydrolytic pathway of cystic fibrosis transmembrane conductance regulator ion channel gating
    • Aleksandrov, A.A., X. Chang, L. Aleksandrov, and J.R. Riordan. 2000. The non-hydrolytic pathway of cystic fibrosis transmembrane conductance regulator ion channel gating. J. Physiol. 528:259-265.
    • (2000) J. Physiol , vol.528 , pp. 259-265
    • Aleksandrov, A.A.1    Chang, X.2    Aleksandrov, L.3    Riordan, J.R.4
  • 4
    • 67649659825 scopus 로고    scopus 로고
    • Relationship between nucleotide binding and ion channel gating in cystic fibrosis transmembrane conductance regulator
    • Aleksandrov, A.A., L. Cui, and J.R. Riordan. 2009. Relationship between nucleotide binding and ion channel gating in cystic fibrosis transmembrane conductance regulator. J. Physiol. 587:2875-2886.
    • (2009) J. Physiol , vol.587 , pp. 2875-2886
    • Aleksandrov, A.A.1    Cui, L.2    Riordan, J.R.3
  • 5
    • 13444274310 scopus 로고    scopus 로고
    • Gating of acetylcholine receptor channels: Brownian motion across a broad transition state
    • Auerbach, A. 2005. Gating of acetylcholine receptor channels: brownian motion across a broad transition state. Proc. Natl. Acad. Sci. USA. 102:1408-1412.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1408-1412
    • Auerbach, A.1
  • 6
    • 36549084005 scopus 로고    scopus 로고
    • How to turn the reaction coordinate into time
    • Auerbach, A. 2007. How to turn the reaction coordinate into time. J. Gen. Physiol. 130:543-546.
    • (2007) J. Gen. Physiol , vol.130 , pp. 543-546
    • Auerbach, A.1
  • 7
    • 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.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 87-92
    • Chakrapani, S.1    Auerbach, A.2
  • 8
    • 1842686239 scopus 로고    scopus 로고
    • Gating dynamics of the acetylcholine receptor extracellular domain
    • Chakrapani, S., T.D. Bailey, and A. Auerbach. 2004. Gating dynamics of the acetylcholine receptor extracellular domain. J. Gen. Physiol. 123:341-356.
    • (2004) J. Gen. Physiol , vol.123 , pp. 341-356
    • Chakrapani, S.1    Bailey, T.D.2    Auerbach, A.3
  • 9
    • 42049096734 scopus 로고    scopus 로고
    • CLC-0 and CFTR: Chloride channels evolved from transporters
    • Chen, T.Y., and T.C. Hwang. 2008. CLC-0 and CFTR: chloride channels evolved from transporters. Physiol. Rev. 88:351-387.
    • (2008) Physiol. Rev , vol.88 , pp. 351-387
    • Chen, T.Y.1    Hwang, T.C.2
  • 10
    • 0029745419 scopus 로고    scopus 로고
    • Nonequilibrium gating and voltage dependence of the ClC-0 Cl- channel
    • Chen, T.Y., and C. Miller. 1996. Nonequilibrium gating and voltage dependence of the ClC-0 Cl- channel. J. Gen. Physiol. 108:237-250.
    • (1996) J. Gen. Physiol , vol.108 , pp. 237-250
    • Chen, T.Y.1    Miller, C.2
  • 11
    • 0242415285 scopus 로고    scopus 로고
    • Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels
    • Chen, T.Y., M.F. Chen, and C.W. Lin. 2003. Electrostatic control and chloride regulation of the fast gating of ClC-0 chloride channels. J. Gen. Physiol. 122:641-651.
    • (2003) J. Gen. Physiol , vol.122 , pp. 641-651
    • Chen, T.Y.1    Chen, M.F.2    Lin, C.W.3
  • 12
    • 53249130652 scopus 로고    scopus 로고
    • The twain shall meet: Channels, transporters and things between. Meeting on Membrane Transport in Flux: the Ambiguous Interface Between Channels and Pumps
    • 9:960-965
    • Csanády, L., and J.A. Mindell. 2008. The twain shall meet: channels, transporters and things between. Meeting on Membrane Transport in Flux: the Ambiguous Interface Between Channels and Pumps. EMBO Rep. 9:960-965.
    • (2008) EMBO Rep
    • Csanády, L.1    Mindell, J.A.2
  • 13
    • 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.
    • (2006) J. Gen. Physiol , vol.128 , pp. 523-533
    • Csanády, L.1    Nairn, A.C.2    Gadsby, D.C.3
  • 14
    • 0037197654 scopus 로고    scopus 로고
    • Structure of the transition state of gating in the acetylcholine receptor channel pore: A phi-value analysis
    • Cymes, G.D., C. Grosman, and A. Auerbach. 2002. Structure of the transition state of gating in the acetylcholine receptor channel pore: a phi-value analysis. Biochemistry. 41:5548-5555.
    • (2002) Biochemistry , vol.41 , pp. 5548-5555
    • Cymes, G.D.1    Grosman, C.2    Auerbach, A.3
  • 15
    • 67349185408 scopus 로고    scopus 로고
    • Ion channels versus ion pumps: The principal difference, in principle
    • Gadsby, D.C. 2009. Ion channels versus ion pumps: the principal difference, in principle. Nat. Rev. Mol. Cell Biol. 10:344-352.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 344-352
    • Gadsby, D.C.1
  • 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.
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanády, L.3
  • 17
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • Grosman, C., M. Zhou, and A. Auerbach. 2000. Mapping the conformational wave of acetylcholine receptor channel gating. Nature. 403:773-776.
    • (2000) Nature , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 18
    • 0001060616 scopus 로고
    • Structure-energy relations, reaction mechanism, and disparity of progress of concerted reaction events
    • Grunwald, E. 1985. Structure-energy relations, reaction mechanism, and disparity of progress of concerted reaction events. J. Am. Chem. Soc. 107:125-133.
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 125-133
    • Grunwald, E.1
  • 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.
    • (1995) Cell , vol.82 , pp. 231-239
    • Gunderson, K.L.1    Kopito, R.R.2
  • 21
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure and mechanism-an overview
    • Higgins, C.F. 2001. ABC transporters: physiology, structure and mechanism-an overview. Res. Microbiol. 152:205-210.
    • (2001) Res. Microbiol , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 22
    • 65749102092 scopus 로고    scopus 로고
    • Gating of the CFTR Clchannel by ATP-driven nucleotide-binding domain dimerisation
    • Hwang, T.C., and D.N. Sheppard. 2009. Gating of the CFTR Clchannel by ATP-driven nucleotide-binding domain dimerisation. J. Physiol. 587:2151-2161.
    • (2009) J. Physiol , vol.587 , pp. 2151-2161
    • Hwang, T.C.1    Sheppard, D.N.2
  • 23
    • 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.
    • (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
  • 24
    • 0030668944 scopus 로고    scopus 로고
    • Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis
    • Ishihara, H., and M.J. Welsh. 1997. Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis. Am. J. Physiol. 273:C1278-C1289.
    • (1997) Am. J. Physiol , vol.273
    • Ishihara, H.1    Welsh, M.J.2
  • 25
    • 0038711772 scopus 로고    scopus 로고
    • Janas, E., M. Hofacker, M. Chen, S. Gompf, C. van der Does, and R. Tampé. 2003. The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 278:26862-26869.
    • Janas, E., M. Hofacker, M. Chen, S. Gompf, C. van der Does, and R. Tampé. 2003. The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 278:26862-26869.
  • 26
    • 49449090405 scopus 로고    scopus 로고
    • The ClC-0 chloride channel is a 'broken' Cl-/H+ antiporter
    • Lísal, J., and M. Maduke. 2008. The ClC-0 chloride channel is a 'broken' Cl-/H+ antiporter. Nat. Struct. Mol. Biol. 15:805-810.
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 805-810
    • Lísal, J.1    Maduke, M.2
  • 27
    • 33947306589 scopus 로고
    • Theoretical relations among rate constants, barriers, and Brønsted slopes of chemical reactions
    • Marcus, R.A. 1968. Theoretical relations among rate constants, barriers, and Brønsted slopes of chemical reactions. J. Phys. Chem. 72:891-899.
    • (1968) J. Phys. Chem , vol.72 , pp. 891-899
    • Marcus, R.A.1
  • 28
    • 33645296826 scopus 로고    scopus 로고
    • ClC chloride channels viewed through a transporter lens
    • Miller, C. 2006. ClC chloride channels viewed through a transporter lens. Nature. 440:484-489.
    • (2006) Nature , vol.440 , pp. 484-489
    • Miller, C.1
  • 29
    • 27744443715 scopus 로고    scopus 로고
    • Plasticity of acetylcholine receptor gating motions via rate-energy relationships
    • Mitra, A., R. Tascione, A. Auerbach, and S. Licht. 2005. Plasticity of acetylcholine receptor gating motions via rate-energy relationships. Biophys. J. 89:3071-3078.
    • (2005) Biophys. J , vol.89 , pp. 3071-3078
    • Mitra, A.1    Tascione, R.2    Auerbach, A.3    Licht, S.4
  • 30
    • 0037077296 scopus 로고    scopus 로고
    • Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters
    • Moody, J.E., L. Millen, D. Binns, J.F. Hunt, and P.J. Thomas. 2002. Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 277:21111-21114.
    • (2002) J. Biol. Chem , vol.277 , pp. 21111-21114
    • Moody, J.E.1    Millen, L.2    Binns, D.3    Hunt, J.F.4    Thomas, P.J.5
  • 31
  • 32
    • 0028924935 scopus 로고
    • Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion
    • Pusch, M., U. Ludewig, A. Rehfeldt, and T.J. Jentsch. 1995. Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion. Nature. 373:527-531.
    • (1995) Nature , vol.373 , pp. 527-531
    • Pusch, M.1    Ludewig, U.2    Rehfeldt, A.3    Jentsch, T.J.4
  • 33
    • 0025270712 scopus 로고
    • Steady-state coupling of ionchannel conformations to a transmembrane ion gradient
    • Richard, E.A., and C. Miller. 1990. Steady-state coupling of ionchannel conformations to a transmembrane ion gradient. Science. 247:1208-1210.
    • (1990) Science , vol.247 , pp. 1208-1210
    • Richard, E.A.1    Miller, C.2
  • 36
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P.C., N. Karpowich, L. Millen, J.E. Moody, J. Rosen, P.J. Thomas, and J.F. Hunt. 2002. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell. 10:139-149.
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 38
    • 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.
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.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.
    • (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
    • 27744499937 scopus 로고    scopus 로고
    • Phi-value analysis of a linear, sequential reaction mechanism: Theory and application to ion channel gating
    • Zhou, Y., J.E. Pearson, and A. Auerbach. 2005. Phi-value analysis of a linear, sequential reaction mechanism: theory and application to ion channel gating. Biophys. J. 89:3680-3685.
    • (2005) Biophys. J , vol.89 , pp. 3680-3685
    • Zhou, Y.1    Pearson, J.E.2    Auerbach, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.