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Volumn 63, Issue , 2003, Pages 211-241

The voltage sensor and the gate in ion channels

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; HISTIDINE; ION CHANNEL; MEMBRANE PROTEIN;

EID: 0037282379     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(03)63009-3     Document Type: Review
Times cited : (37)

References (70)
  • 2
    • 0017796425 scopus 로고
    • Gating currents and charge movements in excitable membranes
    • Almers, W. (1978). Gating currents and charge movements in excitable membranes. Rev. Physiol. Biochem. Pharmacol. 82, 96-190.
    • (1978) Rev. Physiol. Biochem. Pharmacol. , vol.82 , pp. 96-190
    • Almers, W.1
  • 3
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach, C., Marti, T., Khorana, H. G., and Hubbell, W. L. (1990). Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science 248, 1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 4
    • 0015142234 scopus 로고
    • Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons
    • Armstrong, C. M. (1971). Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons. J. Gen. Physiol. 58, 413-437.
    • (1971) J. Gen. Physiol. , vol.58 , pp. 413-437
    • Armstrong, C.M.1
  • 5
    • 0003205737 scopus 로고    scopus 로고
    • Probing the electric field in the Shaker potassium channel
    • Asamoah, O. K., Bezanilla, F., and Loew, L. (2002). Probing the electric field in the Shaker potassium channel. Biophys. J. 82, 233a.
    • (2002) Biophys. J. , vol.82
    • Asamoah, O.K.1    Bezanilla, F.2    Loew, L.3
  • 7
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla, F. (2000). The voltage sensor in voltage-dependent ion channels. Physiol. Rev. 80, 555-592.
    • (2000) Physiol. Rev. , vol.80 , pp. 555-592
    • Bezanilla, F.1
  • 10
    • 0030840167 scopus 로고    scopus 로고
    • + channel with fluorescence
    • + channel with fluorescence. Neuron 19, 1127-1140.
    • (1997) Neuron , vol.19 , pp. 1127-1140
    • Cha, A.1    Bezanilla, F.2
  • 12
    • 0033576580 scopus 로고    scopus 로고
    • Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
    • Cha, A., Snyder, G. E., Selvin, P. R., and Bezanilla, F. (1999). Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature 402, 809-813.
    • (1999) Nature , vol.402 , pp. 809-813
    • Cha, A.1    Snyder, G.E.2    Selvin, P.R.3    Bezanilla, F.4
  • 13
    • 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., VanDongen, H. M., and VanDongen, A. M. (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
  • 15
    • 0029861318 scopus 로고    scopus 로고
    • + channel gating in nerve axons revisited
    • + channel gating in nerve axons revisited. J. Membrane Biol. 153, 195-201.
    • (1996) J. Membrane Biol. , vol.153 , pp. 195-201
    • Clay, J.R.1
  • 16
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in α-helices: Analysis by variation of side chain structure
    • Columbus, L., Kálai, T., Jekö, J., Hideg, K., and Hubbell, W. L. (2001). Molecular motion of spin labeled side chains in α-helices: Analysis by variation of side chain structure. Biochemistry 40, 3828-3846.
    • (2001) Biochemistry , vol.40 , pp. 3828-3846
    • Columbus, L.1    Kálai, T.2    Jekö, J.3    Hideg, K.4    Hubbell, W.L.5
  • 17
    • 0024346408 scopus 로고
    • Quantal charge redistribution accompanying the structural transitions of sodium channels
    • Conti, F., and Stuhmer, W. (1989). Quantal charge redistribution accompanying the structural transitions of sodium channels. Eur. Biophys. J. 17, 53-59.
    • (1989) Eur. Biophys. J. , vol.17 , pp. 53-59
    • Conti, F.1    Stuhmer, W.2
  • 18
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D., Cuello, L., and Perozo, E. (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.1    Cuello, L.2    Perozo, E.3
  • 21
    • 0026519665 scopus 로고
    • + channel correlate with occupancy of the pore
    • + 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
  • 23
    • 0033576706 scopus 로고    scopus 로고
    • Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel
    • Glauner, K. S., Mannuzzu, L. M., Gandhi, C. S., and Isacoff, E. Y (1999). Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel. Nature 402, 813-817.
    • (1999) Nature , vol.402 , pp. 813-817
    • Glauner, K.S.1    Mannuzzu, L.M.2    Gandhi, C.S.3    Isacoff, E.Y.4
  • 26
    • 0033543132 scopus 로고    scopus 로고
    • Structure of the KcsA potassium channel from Streptomyces lividans: A site-directed spin labeling study of the second transmembrane segment
    • Gross, A., Columbus, L., Hideg, K., Altenbach, C., and Hubbell, W. L. (1999). Structure of the KcsA potassium channel from Streptomyces lividans: a site-directed spin labeling study of the second transmembrane segment. Biochemistry 38, 10324-10335.
    • (1999) Biochemistry , vol.38 , pp. 10324-10335
    • Gross, A.1    Columbus, L.2    Hideg, K.3    Altenbach, C.4    Hubbell, W.L.5
  • 29
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin, A. L., and Huxley, A. F. (1952). A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 117, 500-544.
    • (1952) J. Physiol. , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 30
    • 0001300193 scopus 로고
    • Spin label oxymetry
    • L.J.a.R. Berliner, Ed. Plenum, New York
    • Hyde, J. S., and Subczynski, W. K. (1989). Spin label oxymetry. In Biological Magnetic Resonance, Vol. 8 (L.J.a.R. Berliner, Ed.), pp. 399-425. Plenum, New York.
    • (1989) Biological Magnetic Resonance , vol.8 , pp. 399-425
    • Hyde, J.S.1    Subczynski, W.K.2
  • 31
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., and MacKinnon, R. (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
  • 34
    • 0001273328 scopus 로고    scopus 로고
    • Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels
    • Li-Smerin, Y., and Swartz, K. (2001). Helical structure of the COOH terminus of S3 and its contribution to the gating modifier toxin receptor in voltage-gated ion channels. J. Gen. Physiol. 113, 415-423.
    • (2001) J. Gen. Physiol. , vol.113 , pp. 415-423
    • Li-Smerin, Y.1    Swartz, K.2
  • 37
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • Liu, Y. S., Sompornpisut, P., and Perozo, E. (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
  • 40
    • 0030059224 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • Mannuzzu, L. M., Moronne, M. M., and Isacoff, E. Y. (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
  • 41
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996). Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35, 7692-7704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 42
    • 0032725268 scopus 로고    scopus 로고
    • Exploring the open pore of the potassium channel from Streptomyces lividans
    • Meuser, D., Splitt, H., Wagner, R., and Schrempf, H. (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
  • 49
    • 0034030261 scopus 로고    scopus 로고
    • Gating and flickery block differentially affected by rubidium in homomeric KCNQ1 and heteromeric KCNQ1/KCNE1 potassium channels
    • Pusch, M., Bertorello, L., and Conti, F. (2000). Gating and flickery block differentially affected by rubidium in homomeric KCNQ1 and heteromeric KCNQ1/KCNE1 potassium channels. Biophys. J. 78, 211-226.
    • (2000) Biophys. J. , vol.78 , pp. 211-226
    • Pusch, M.1    Bertorello, L.2    Conti, F.3
  • 50
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein, M. D., and Shin, Y. K. (1995). Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. USA 92, 8239-8243.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 51
    • 0035861457 scopus 로고    scopus 로고
    • A prokaryotic voltage-gated sodium channel
    • Ren, D., Navarro, B., Xu, H., Yue, L., Shi, Q., and Clapham, D. E. (2001). A prokaryotic voltage-gated sodium channel. Science 294, 2372-2375.
    • (2001) Science , vol.294 , pp. 2372-2375
    • Ren, D.1    Navarro, B.2    Xu, H.3    Yue, L.4    Shi, Q.5    Clapham, D.E.6
  • 52
    • 0036355083 scopus 로고    scopus 로고
    • What can be deduced about the structure of Shaker from available data?
    • Roux, B. (2002). What can be deduced about the structure of Shaker from available data? Novartis Found. Symp. 245, 84-101.
    • (2002) Novartis Found. Symp. , vol.245 , pp. 84-101
    • Roux, B.1
  • 53
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N. E., McCormack, K., Tanouye, M. A., and Sigworth, F. J. (1992). The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255, 1712-1715.
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 54
    • 0028841033 scopus 로고
    • A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans
    • Schrempf, H., Schmidt, O., Kummerlen, R., Hinnah, S., Muller, D., Betzler, M., Steinkamp, T., and Wagner, R. (1995). A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBOJ. 14, 5170-5178.
    • (1995) EMBO J. , vol.14 , pp. 5170-5178
    • Schrempf, H.1    Schmidt, O.2    Kummerlen, R.3    Hinnah, S.4    Muller, D.5    Betzler, M.6    Steinkamp, T.7    Wagner, R.8
  • 57
    • 0026356520 scopus 로고
    • Permeant ion effects on the gating kinetics of the type-L potassium channel in mouse lymphocytes
    • Shapiro, M. S., and Decoursey, T. E. (1991). Permeant ion effects on the gating kinetics of the type-L potassium channel in mouse lymphocytes. J. Gen. Physiol. 97, 1251-1278.
    • (1991) J. Gen. Physiol. , vol.97 , pp. 1251-1278
    • Shapiro, M.S.1    Decoursey, T.E.2
  • 58
    • 0028233117 scopus 로고
    • Gating current noise produced by elementary transition in Shaker potassium channels
    • Sigg, D., Stefani, E., and Bezanilla, F. (1994). Gating current noise produced by elementary transition in Shaker potassium channels. Science 264, 578-582.
    • (1994) Science , vol.264 , pp. 578-582
    • Sigg, D.1    Stefani, E.2    Bezanilla, F.3
  • 59
    • 0031015351 scopus 로고    scopus 로고
    • Total charge movement per channel. The relation between gating displacement and the voltage sensitivity of activation
    • Sigg, D., and Bezanilla, F. (1997). Total charge movement per channel. The relation between gating displacement and the voltage sensitivity of activation. J. Gen. Physiol. 109, 27-39.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 27-39
    • Sigg, D.1    Bezanilla, F.2
  • 60
    • 0034759492 scopus 로고    scopus 로고
    • Calculation of rigid-body conformational changes using restraint-driven Cartesian transformations
    • Sompornpisut, P., Liu, Y.-S., and Perozo, E. (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
  • 61
    • 0024535492 scopus 로고
    • Rubidium ions and the gating of delayed rectifier potassium channels of frog skeletal-muscle
    • Spruce, A. E., Standen, N. B., and Stanfield, P. R. (1989). Rubidium ions and the gating of delayed rectifier potassium channels of frog skeletal-muscle. J. Physiol. (London) 411, 597-610.
    • (1989) J. Physiol. (London) , vol.411 , pp. 597-610
    • Spruce, A.E.1    Standen, N.B.2    Stanfield, P.R.3
  • 63
    • 0035039731 scopus 로고    scopus 로고
    • Histidine scanning mutagenesis of basic residues of the S4 segment of the Shaker K channel
    • Starace, D. M., and Bezanilla, F. (2001). Histidine scanning mutagenesis of basic residues of the S4 segment of the Shaker K channel. J. Gen. Physiol. 117, 469-490.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 469-490
    • Starace, D.M.1    Bezanilla, F.2
  • 68
    • 0029084477 scopus 로고
    • Evidence for voltage-dependent S4 movement in sodium channels
    • Yang, N., and Horn, R. (1995). Evidence for voltage-dependent S4 movement in sodium channels. Neuron 15, 213-218.
    • (1995) Neuron , vol.15 , pp. 213-218
    • Yang, N.1    Horn, R.2
  • 69
    • 0029845542 scopus 로고    scopus 로고
    • Measurement of the movement of the S4 segment during activation of a voltage-gated potassium channel
    • Yusaf, S. P., Wray, D., and Sivaprasadarao, A. (1996). Measurement of the movement of the S4 segment during activation of a voltage-gated potassium channel. Pflugers Arch. Eur. J. Physiol. 433, 91-97.
    • (1996) Pflugers Arch. Eur. J. Physiol. , vol.433 , pp. 91-97
    • Yusaf, S.P.1    Wray, D.2    Sivaprasadarao, A.3
  • 70
    • 0030818830 scopus 로고    scopus 로고
    • Selectivity changes during activation of mutant Shaker potassium channels
    • Zheng, J., and Sigworth, F. J. (1997). Selectivity changes during activation of mutant Shaker potassium channels. J. Gen. Physiol. 110, 101-117.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 101-117
    • Zheng, J.1    Sigworth, F.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.