메뉴 건너뛰기




Volumn 128, Issue 5, 2006, Pages 569-581

Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; POTASSIUM CHANNEL; PROTEIN KCSA; PROTEIN TM2; TETRAMETHYLRHODAMINE ETHYL ESTER; TROPOMYOSIN; UNCLASSIFIED DRUG;

EID: 33750530193     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200609638     Document Type: Article
Times cited : (87)

References (56)
  • 1
    • 2942651050 scopus 로고    scopus 로고
    • Detecting rearrangements of shaker and NaChBac in real-time with fluorescence spectroscopy in patch-clamped mammalian cells
    • Blunck, R., D.M. Starace, A.M. Correa, and F. Bezanilla. 2004. Detecting rearrangements of shaker and NaChBac in real-time with fluorescence spectroscopy in patch-clamped mammalian cells. Biophys. J. 86:3966-3980.
    • (2004) Biophys. J. , vol.86 , pp. 3966-3980
    • Blunck, R.1    Starace, D.M.2    Correa, A.M.3    Bezanilla, F.4
  • 2
    • 0036703631 scopus 로고    scopus 로고
    • Localization of the activation gate for small conductance Ca2+-activated K+ channels
    • Bruening-Wright, A., M.A. Schumacher, J.P. Adelman, and J. Maylie. 2002. Localization of the activation gate for small conductance Ca2+-activated K+ channels. J. Neurosci. 22:6499-6506.
    • (2002) J. Neurosci. , vol.22 , pp. 6499-6506
    • Bruening-Wright, A.1    Schumacher, M.A.2    Adelman, J.P.3    Maylie, J.4
  • 3
    • 0030840167 scopus 로고    scopus 로고
    • Characterizing voltage-dependent conformational changes in the Shaker K+ channel with fluorescence
    • Cha, A., and F. Bezanilla. 1997. Characterizing voltage-dependent conformational changes in the Shaker K+ channel with fluorescence. Neuron. 19:1127-1140.
    • (1997) Neuron , vol.19 , pp. 1127-1140
    • Cha, A.1    Bezanilla, F.2
  • 4
    • 0031022168 scopus 로고    scopus 로고
    • Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating
    • Chapman, M.L., H.M. VanDongen, and A.M. VanDongen. 1997. Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating. Biophys. J. 72:708-719.
    • (1997) Biophys. J. , vol.72 , pp. 708-719
    • Chapman, M.L.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 6
    • 0347379835 scopus 로고    scopus 로고
    • The selectivity filter may act as the agonist-activated gate in the G protein-activated Kir3.1/Kir3.4 K+ channel
    • Claydon, T.W., S.Y. Makary, K.M. Dibb, and M.R. Boyett. 2003. The selectivity filter may act as the agonist-activated gate in the G protein-activated Kir3.1/Kir3.4 K+ channel. J. Biol. Chem. 278:50654-50663.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50654-50663
    • Claydon, T.W.1    Makary, S.Y.2    Dibb, K.M.3    Boyett, M.R.4
  • 8
    • 0030745896 scopus 로고    scopus 로고
    • Structural dynamics of the Streptomyces lividans K+ channel (SKC1): Oligomeric stoichiometry and stability
    • Cortes, D.M., and E. Perozo. 1997. Structural dynamics of the Streptomyces lividans K+ channel (SKC1): oligomeric stoichiometry and stability. Biochemistry. 36:10343-10352.
    • (1997) Biochemistry , vol.36 , pp. 10343-10352
    • Cortes, D.M.1    Perozo, E.2
  • 9
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D.M., L.G. Cuello, and E. Perozo. 2001. Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117:165-180.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 10
    • 0032502286 scopus 로고    scopus 로고
    • pH-dependent gating in the Streptomyces lividans K+ channel
    • Cuello, L.G., J.G. Romero, D.M. Cortes, and E. Perozo. 1998. pH-dependent gating in the Streptomyces lividans K+ channel. Biochemistry. 37:3229-3236.
    • (1998) Biochemistry , vol.37 , pp. 3229-3236
    • Cuello, L.G.1    Romero, J.G.2    Cortes, D.M.3    Perozo, E.4
  • 11
    • 1842740890 scopus 로고    scopus 로고
    • Voltage-dependent gating of hyperpolarization-activated, cyclic nucleotide-gated pacemaker channels: Molecular coupling between the S4-S5 and C-linkers
    • Decher, N., J. Chen, and M.C. Sanguinetti. 2004. Voltage-dependent gating of hyperpolarization-activated, cyclic nucleotide-gated pacemaker channels: molecular coupling between the S4-S5 and C-linkers. J. Biol. Chem. 279:13859-13865.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13859-13865
    • Decher, N.1    Chen, J.2    Sanguinetti, M.C.3
  • 12
    • 0035923745 scopus 로고    scopus 로고
    • Tight steric closure at the intracellular activation gate of a voltage-gated K(+) channel
    • Del Camino, D., and G. Yellen. 2001. Tight steric closure at the intracellular activation gate of a voltage-gated K(+) channel. Neuron. 32:649-656.
    • (2001) Neuron , vol.32 , pp. 649-656
    • Del Camino, D.1    Yellen, G.2
  • 13
    • 0034688285 scopus 로고    scopus 로고
    • Blocker protection in the pore of a voltage-gated K+ channel and its structural implications
    • Del Camino, D., M. Holmgren, Y. Liu, and G. Yellen. 2000. Blocker protection in the pore of a voltage-gated K+ channel and its structural implications. Nature. 403:321-325.
    • (2000) Nature , vol.403 , pp. 321-325
    • Del Camino, D.1    Holmgren, M.2    Liu, Y.3    Yellen, G.4
  • 14
    • 0024438904 scopus 로고
    • Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels
    • Delcour, A.H., B. Martinac, J. Adler, and C. Kung. 1989. Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels. Biophys. J. 56:631-636.
    • (1989) Biophys. J. , vol.56 , pp. 631-636
    • Delcour, A.H.1    Martinac, B.2    Adler, J.3    Kung, C.4
  • 15
    • 0026519665 scopus 로고
    • Ion effects on gating of the Ca(2+)-activated K+ channel correlate with occupancy of the pore
    • Demo, S.D., and G. Yellen. 1992. Ion effects on gating of the Ca(2+)-activated K+ channel correlate with occupancy of the pore. Biophys. J. 61:639-648.
    • (1992) Biophys. J. , vol.61 , pp. 639-648
    • Demo, S.D.1    Yellen, G.2
  • 17
    • 0000378986 scopus 로고
    • Photophysics of indole-derivatives - Experimental resolution of la and Lb transitions and comparison with theory
    • Eftink, M.R., L.A. Selvidge, P.R. Callis, and A.A. Rehms. 1990. Photophysics of indole-derivatives - experimental resolution of la and Lb transitions and comparison with theory. J. Phys. Chem. 94:3469-3479.
    • (1990) J. Phys. Chem. , vol.94 , pp. 3469-3479
    • Eftink, M.R.1    Selvidge, L.A.2    Callis, P.R.3    Rehms, A.A.4
  • 18
    • 0034977038 scopus 로고    scopus 로고
    • Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels
    • Flynn, G.E., and W.N. Zagotta. 2001. Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels. Neuron. 30:689-698.
    • (2001) Neuron , vol.30 , pp. 689-698
    • Flynn, G.E.1    Zagotta, W.N.2
  • 19
    • 0032875483 scopus 로고    scopus 로고
    • Single Streptomyces lividans K(+) channels: Functional asymmetries and sidedness of proton activation
    • Heginbotham, L., M. LeMasurier, L. Kolmakova-Partensky, and C. Miller. 1999. Single Streptomyces lividans K(+) channels: functional asymmetries and sidedness of proton activation. J. Gen. Physiol. 114:551-560.
    • (1999) J. Gen. Physiol. , vol.114 , pp. 551-560
    • Heginbotham, L.1    Lemasurier, M.2    Kolmakova-Partensky, L.3    Miller, C.4
  • 20
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon. 2002a. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 23
    • 0038752614 scopus 로고    scopus 로고
    • The principle of gating charge movement in a voltage-dependent K(+) channel
    • Jiang, Y., V. Ruta, J. Chen, A. Lee, and R. MacKinnon. 2003b. The principle of gating charge movement in a voltage-dependent K(+) channel. Nature. 423:42-48.
    • (2003) Nature , vol.423 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Chen, J.3    Lee, A.4    MacKinnon, R.5
  • 24
    • 0037387189 scopus 로고    scopus 로고
    • Potassium channel gating observed with site-directed mass tagging
    • Kelly, B.L., and A. Gross. 2003. Potassium channel gating observed with site-directed mass tagging. Nat. Struct. Biol. 10:280-284.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 280-284
    • Kelly, B.L.1    Gross, A.2
  • 27
    • 0030795112 scopus 로고    scopus 로고
    • Gated access to the pore of a voltage-dependent K+ channel
    • Liu, Y., M. Holmgren, M.E. Jurman, and G. Yellen. 1997. Gated access to the pore of a voltage-dependent K+ channel. Neuron. 19:175-184.
    • (1997) Neuron , vol.19 , pp. 175-184
    • Liu, Y.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 28
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • Liu, Y.S., P. Sompornpisut, and E. Perozo. 2001. Structure of the KcsA channel intracellular gate in the open state. Nat. Struct. Biol. 8:883-887.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 883-887
    • Liu, Y.S.1    Sompornpisut, P.2    Perozo, E.3
  • 29
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S.B., E.B. Campbell, and R. MacKinnon. 2005. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science. 309:897-903.
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 30
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • Lopez-Barneo, J., T. Hoshi, S.H. Heinemann, and R.W. Aldrich. 1993. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels. 1:61-71.
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • Lopez-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 31
    • 0035119276 scopus 로고    scopus 로고
    • Probing ion permeation and gating in a K+ channel with backbone mutations in the selectivity filter
    • Lu, T., A.Y. Ting, J. Mainland, L.Y. Jan, P.G. Schultz, and J. Yang. 2001. Probing ion permeation and gating in a K+ channel with backbone mutations in the selectivity filter. Nat. Neurosci. 4:239-246.
    • (2001) Nat. Neurosci. , vol.4 , pp. 239-246
    • Lu, T.1    Ting, A.Y.2    Mainland, J.3    Jan, L.Y.4    Schultz, P.G.5    Yang, J.6
  • 32
    • 0036846783 scopus 로고    scopus 로고
    • Coupling between voltage sensors and activation gate in voltage-gated K+ channels
    • Lu, Z., A.M. Klem, and Y. Ramu. 2002. Coupling between voltage sensors and activation gate in voltage-gated K+ channels. J. Gen. Physiol. 120:663-676.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 663-676
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 33
    • 0030059224 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • Mannuzzu, L.M., M.M. Moronne, and E.Y. Isacoff. 1996. Direct physical measure of conformational rearrangement underlying potassium channel gating. Science. 271:213-216.
    • (1996) Science , vol.271 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 34
    • 0344494656 scopus 로고    scopus 로고
    • Inter- and intramolecular fluorescence quenching of organic dyes by tryptophan
    • Marme, N., J.P. Knemeyer, M. Sauer, and J. Wolfrum. 2003. Inter- and intramolecular fluorescence quenching of organic dyes by tryptophan. Bioconjug. Chem. 14:1133-1139.
    • (2003) Bioconjug. Chem. , vol.14 , pp. 1133-1139
    • Marme, N.1    Knemeyer, J.P.2    Sauer, M.3    Wolfrum, J.4
  • 36
    • 0032725268 scopus 로고    scopus 로고
    • Exploring the open pore of the potassium channel from Streptomyces lividans
    • Meuser, D., H. Splitt, R. Wagner, and H. Schrempf. 1999. Exploring the open pore of the potassium channel from Streptomyces lividans. FEBS Lett. 462:447-452.
    • (1999) FEBS Lett. , vol.462 , pp. 447-452
    • Meuser, D.1    Splitt, H.2    Wagner, R.3    Schrempf, H.4
  • 37
    • 0034805579 scopus 로고    scopus 로고
    • Bilayer reconstitution of voltage-dependent ion channels using a microfabricated silicon chip
    • Pantoja, R., D. Sigg, R. Blunck, F. Bezanilla, and J.R. Heath. 2001. Bilayer reconstitution of voltage-dependent ion channels using a microfabricated silicon chip. Biophys. J. 81:2389-2394.
    • (2001) Biophys. J. , vol.81 , pp. 2389-2394
    • Pantoja, R.1    Sigg, D.2    Blunck, R.3    Bezanilla, F.4    Heath, J.R.5
  • 38
    • 23244467740 scopus 로고    scopus 로고
    • The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel
    • Pavlov, E., C. Bladen, R. Winkfein, C. Diao, P. Dhaliwal, and R. French. 2005. The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel. Biophys. J. 89:232-242.
    • (2005) Biophys. J. , vol.89 , pp. 232-242
    • Pavlov, E.1    Bladen, C.2    Winkfein, R.3    Diao, C.4    Dhaliwal, P.5    French, R.6
  • 39
    • 2642701712 scopus 로고    scopus 로고
    • Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy
    • Perozo, E., D.M. Cortes, and L.G. Cuello. 1998. Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy. Nat. Struct. Biol. 5:459-469.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 459-469
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 40
    • 0033516494 scopus 로고    scopus 로고
    • Structural rearrangements underlying K+-channel activation gating
    • Perozo, E., D.M. Cortes, and L.G. Cuello. 1999. Structural rearrangements underlying K+-channel activation gating. Science. 285:73-78.
    • (1999) Science , vol.285 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 41
    • 0345166926 scopus 로고    scopus 로고
    • Ligand-induced closure of inward rectifier Kir6.2 channels traps spermine in the pore
    • Phillips, L.R., and C.G. Nichols. 2003. Ligand-induced closure of inward rectifier Kir6.2 channels traps spermine in the pore. J. Gen. Physiol. 122:795-804.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 795-804
    • Phillips, L.R.1    Nichols, C.G.2
  • 42
    • 0034774587 scopus 로고    scopus 로고
    • Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel
    • Proks, P., C.E. Capener, P. Jones, and F.M. Ashcroft. 2001. Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel. J. Gen. Physiol. 118:341-353.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 341-353
    • Proks, P.1    Capener, C.E.2    Jones, P.3    Ashcroft, F.M.4
  • 43
    • 0037223669 scopus 로고    scopus 로고
    • The ligand-sensitive gate of a potassium channel lies close to the selectivity filter
    • Proks, P., J.F. Antcliff, and F.M. Ashcroft. 2003. The ligand-sensitive gate of a potassium channel lies close to the selectivity filter. EMBO Rep. 4:70-75.
    • (2003) EMBO Rep. , vol.4 , pp. 70-75
    • Proks, P.1    Antcliff, J.F.2    Ashcroft, F.M.3
  • 44
    • 0033082093 scopus 로고    scopus 로고
    • Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes
    • Sanguinetti, M.C., and Q.P. Xu. 1999. Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes. J. Physiol. 514(Pt 3):667-675.
    • (1999) J. Physiol. , vol.514 , Issue.PART 3 , pp. 667-675
    • Sanguinetti, M.C.1    Xu, Q.P.2
  • 45
    • 0031952460 scopus 로고    scopus 로고
    • Activation of Shaker potassium channels. II. Kinetics of the V2 mutant channel
    • Schoppa, N.E., and F.J. Sigworth. 1998. Activation of Shaker potassium channels. II. Kinetics of the V2 mutant channel. J. Gen. Physiol. 111:295-311.
    • (1998) J. Gen. Physiol. , vol.111 , pp. 295-311
    • Schoppa, N.E.1    Sigworth, F.J.2
  • 46
    • 0034759492 scopus 로고    scopus 로고
    • Calculation of rigid-body conformational changes using restraint-driven Cartesian transformations
    • Sompornpisut, P., Y.S. Liu, and E. Perozo. 2001. Calculation of rigid-body conformational changes using restraint-driven Cartesian transformations. Biophys. J. 81:2530-2546.
    • (2001) Biophys. J. , vol.81 , pp. 2530-2546
    • Sompornpisut, P.1    Liu, Y.S.2    Perozo, E.3
  • 47
    • 0024535492 scopus 로고
    • Rubidium ions and the gating of delayed rectifier potassium channels of frog skeletal muscle
    • Spruce, A.E., N.B. Standen, and P.R. Stanfield. 1989. Rubidium ions and the gating of delayed rectifier potassium channels of frog skeletal muscle. J. Physiol. 411:597-610.
    • (1989) J. Physiol. , vol.411 , pp. 597-610
    • Spruce, A.E.1    Standen, N.B.2    Stanfield, P.R.3
  • 49
    • 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
  • 50
    • 0019418315 scopus 로고
    • K+ channels close more slowly in the presence of external K+ and Rb+
    • Swenson, R.P., Jr., and C.M. Armstrong. 1981. K+ channels close more slowly in the presence of external K+ and Rb+. Nature. 291:427-429.
    • (1981) Nature , vol.291 , pp. 427-429
    • Swenson Jr., R.P.1    Armstrong, C.M.2
  • 51
    • 1942467020 scopus 로고    scopus 로고
    • Intracellular gate opening in Shaker K+ channels defined by high-affinity metal bridges
    • Webster, S.M., D. Del Camino, J.P. Dekker, and G. Yellen. 2004. Intracellular gate opening in Shaker K+ channels defined by high-affinity metal bridges. Nature. 428:864-868.
    • (2004) Nature , vol.428 , pp. 864-868
    • Webster, S.M.1    Del Camino, D.2    Dekker, J.P.3    Yellen, G.4
  • 52
    • 0042209593 scopus 로고    scopus 로고
    • Localization of PIP2 activation gate in inward rectifier K+ channels
    • Xiao, J., X.G. Zhen, and J. Yang. 2003. Localization of PIP2 activation gate in inward rectifier K+ channels. Nat. Neurosci. 6:811-818.
    • (2003) Nat. Neurosci. , vol.6 , pp. 811-818
    • Xiao, J.1    Zhen, X.G.2    Yang, J.3
  • 53
    • 1842422868 scopus 로고    scopus 로고
    • A gating hinge in Na+ channels; a molecular switch for electrical signaling
    • Zhao, Y., V. Yarov-Yarovoy, T. Scheuer, and W.A. Catterall. 2004. A gating hinge in Na+ channels; a molecular switch for electrical signaling. Neuron. 41:859-865.
    • (2004) Neuron , vol.41 , pp. 859-865
    • Zhao, Y.1    Yarov-Yarovoy, V.2    Scheuer, T.3    Catterall, W.A.4
  • 54
    • 0031718345 scopus 로고    scopus 로고
    • Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels
    • Zheng, J., and F.J. Sigworth. 1998. Intermediate conductances during deactivation of heteromultimeric Shaker potassium channels. J. Gen. Physiol. 112:457-474.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 457-474
    • Zheng, J.1    Sigworth, F.J.2
  • 55
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution
    • Zhou, Y., J.H. Morais-Cabral, A. Kaufman, and R. MacKinnon. 2001. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution. Nature. 414:43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.