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Volumn 40, Issue 3, 2003, Pages 515-525

The orientation and molecular movement of a K+ channel voltage-sensing domain

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; HELIX LOOP HELIX PROTEIN; LIPID; MEMBRANE PROTEIN; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 0344256586     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(03)00646-9     Document Type: Article
Times cited : (109)

References (40)
  • 1
    • 0030175348 scopus 로고    scopus 로고
    • Contribution of the S4 segment to gating charge in the Shaker K+ channel
    • Aggarwal S.K., MacKinnon R. Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron. 16:1996;1169-1177.
    • (1996) Neuron , vol.16 , pp. 1169-1177
    • Aggarwal, S.K.1    Mackinnon, R.2
  • 2
    • 17044460689 scopus 로고    scopus 로고
    • Three transmembrane conformations and sequence-dependent displacement of the S4 domain in shaker K+ channel gating
    • Baker O.S., Larsson H.P., Mannuzzu L.M., Isacoff E.Y. Three transmembrane conformations and sequence-dependent displacement of the S4 domain in shaker K+ channel gating. Neuron. 20:1998;1283-1294.
    • (1998) Neuron , vol.20 , pp. 1283-1294
    • Baker, O.S.1    Larsson, H.P.2    Mannuzzu, L.M.3    Isacoff, E.Y.4
  • 3
    • 0036795297 scopus 로고    scopus 로고
    • Voltage sensor movements
    • Bezanilla F. Voltage sensor movements. J. Gen. Physiol. 120:2002;465-473.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 465-473
    • Bezanilla, F.1
  • 4
    • 0026639440 scopus 로고
    • Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies
    • Careaga C.L., Falke J.J. Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies. Biophys. J. 62:1992;209-216.
    • (1992) Biophys. J. , vol.62 , pp. 209-216
    • Careaga, C.L.1    Falke, J.J.2
  • 5
    • 0041695463 scopus 로고    scopus 로고
    • Answers and questions from the KvAP structures
    • Cohen B.E., Grabe M., Jan L.Y. Answers and questions from the KvAP structures. Neuron. 39:2003;395-400.
    • (2003) Neuron , vol.39 , pp. 395-400
    • Cohen, B.E.1    Grabe, M.2    Jan, L.Y.3
  • 7
    • 0031877384 scopus 로고    scopus 로고
    • Structural models of the transmembrance region of voltage-gated and other K+ channels in open, closed, and inactivated confromations
    • Durell S.R., Hao Y., Guy H.R. Structural models of the transmembrance region of voltage-gated and other K+ channels in open, closed, and inactivated confromations. J. Struct. Biol. 121:1998;263-284.
    • (1998) J. Struct. Biol. , vol.121 , pp. 263-284
    • Durell, S.R.1    Hao, Y.2    Guy, H.R.3
  • 8
    • 0034930982 scopus 로고    scopus 로고
    • S4 charges move close to residues in the pore domain during activation in a K channel
    • Elinder F., Mannikko R., Larsson H.P. S4 charges move close to residues in the pore domain during activation in a K channel. J. Gen. Physiol. 118:2001;1-10.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 1-10
    • Elinder, F.1    Mannikko, R.2    Larsson, H.P.3
  • 9
    • 0036792837 scopus 로고    scopus 로고
    • Molecular models of voltage sensing
    • Gandhi C.S., Isacoff E.Y. Molecular models of voltage sensing. J. Gen. Physiol. 120:2002;455-463.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 455-463
    • Gandhi, C.S.1    Isacoff, E.Y.2
  • 10
    • 0033680734 scopus 로고    scopus 로고
    • Reconstructing voltage sensor-pore interaction from a fluorescence scan of a voltage-gated K+ channel
    • Gandhi C.S., Loots E., Isacoff E.Y. Reconstructing voltage sensor-pore interaction from a fluorescence scan of a voltage-gated K+ channel. Neuron. 27:2000;585-595.
    • (2000) Neuron , vol.27 , pp. 585-595
    • Gandhi, C.S.1    Loots, E.2    Isacoff, E.Y.3
  • 11
    • 0035859893 scopus 로고    scopus 로고
    • Periodic perturbations in Shaker K+ channel gating kinetics by deletions in the S3-S4 linker
    • Gonzalez C., Rosenman E., Bezanilla F., Alvarez O., Latorre R. Periodic perturbations in Shaker K+ channel gating kinetics by deletions in the S3-S4 linker. Proc. Natl. Acad. Sci. USA. 98:2001;9617-9623.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9617-9623
    • Gonzalez, C.1    Rosenman, E.2    Bezanilla, F.3    Alvarez, O.4    Latorre, R.5
  • 12
    • 0002271340 scopus 로고    scopus 로고
    • The lipid-protein interface of a Shaker K(+) channel
    • Hong K.H., Miller C. The lipid-protein interface of a Shaker K(+) channel. J. Gen. Physiol. 115:2000;51-58.
    • (2000) J. Gen. Physiol. , vol.115 , pp. 51-58
    • Hong, K.H.1    Miller, C.2
  • 13
    • 0033811116 scopus 로고    scopus 로고
    • Immobilizing the moving parts of voltage-gated ion channels
    • Horn R., Ding S., Gruber H.J. Immobilizing the moving parts of voltage-gated ion channels. J. Gen. Physiol. 116:2000;461-476.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 461-476
    • Horn, R.1    Ding, S.2    Gruber, H.J.3
  • 14
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi T., Zagotta W.N., Aldrich R.W. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science. 250:1990;533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 15
    • 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., MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:2002;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
  • 17
    • 0038752614 scopus 로고    scopus 로고
    • The principle of gating charge movement in a voltage-dependent K+ channel
    • b
    • Jiang Y., Ruta V., Chen J., Lee A., MacKinnon R. The principle of gating charge movement in a voltage-dependent K+ channel. Nature. 423:2003;42-48. b.
    • (2003) Nature , vol.423 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Chen, J.3    Lee, A.4    Mackinnon, R.5
  • 20
  • 21
    • 0035023528 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., Swartz K.J. 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. 117:2001;205-218.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 205-218
    • Li-Smerin, Y.1    Swartz, K.J.2
  • 22
    • 0033981341 scopus 로고    scopus 로고
    • Alpha-helical structural elements within the voltage-sensing domains of a K(+) channel
    • Li-Smerin Y., Hackos D.H., Swartz K.J. alpha-helical structural elements within the voltage-sensing domains of a K(+) channel. J. Gen. Physiol. 115:2000;33-50.
    • (2000) J. Gen. Physiol. , vol.115 , pp. 33-50
    • Li-Smerin, Y.1    Hackos, D.H.2    Swartz, K.J.3
  • 23
    • 0029990996 scopus 로고    scopus 로고
    • Dynamic rearrangement of the outer mouth of a K+ channel during gating
    • Liu Y., Jurman M.E., Yellen G. Dynamic rearrangement of the outer mouth of a K+ channel during gating. Neuron. 16:1996;859-867.
    • (1996) Neuron , vol.16 , pp. 859-867
    • Liu, Y.1    Jurman, M.E.2    Yellen, G.3
  • 24
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels
    • Lopez-Barneo J., Hoshi T., Heinemann S.H., Aldrich R.W. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels. 1:1993;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
  • 25
    • 0030059224 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • Mannuzzu L.M., Moronne M.M., Isacoff E.Y. Direct physical measure of conformational rearrangement underlying potassium channel gating. Science. 271:1996;213-216.
    • (1996) Science , vol.271 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 26
    • 0032894975 scopus 로고    scopus 로고
    • Helical structure and packing orientation of the S2 segment in the Shaker K+ channel
    • Monks S.A., Needleman D.J., Miller C. Helical structure and packing orientation of the S2 segment in the Shaker K+ channel. J. Gen. Physiol. 113:1999;415-423.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 415-423
    • Monks, S.A.1    Needleman, D.J.2    Miller, C.3
  • 27
    • 0042707714 scopus 로고    scopus 로고
    • Evidence for inter-subunit interactions between S4 and S5 transmembrane segments of the shaker potassium channel
    • Neale E.J., Elliott D.J., Hunter M., Sivaprasadarao A. Evidence for inter-subunit interactions between S4 and S5 transmembrane segments of the shaker potassium channel. J. Biol. Chem. 278:2003;29079-29085.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29079-29085
    • Neale, E.J.1    Elliott, D.J.2    Hunter, M.3    Sivaprasadarao, A.4
  • 28
    • 0027237603 scopus 로고
    • Gating currents from a nonconducting mutant reveal open-closed conformations in Shaker K+ channels
    • Perozo E., MacKinnon R., Bezanilla F., Stefani E. Gating currents from a nonconducting mutant reveal open-closed conformations in Shaker K+ channels. Neuron. 11:1993;353-358.
    • (1993) Neuron , vol.11 , pp. 353-358
    • Perozo, E.1    Mackinnon, R.2    Bezanilla, F.3    Stefani, E.4
  • 29
    • 0028175781 scopus 로고
    • Glycosylation of shaker potassium channel protein in insect cell culture and in Xenopus oocytes
    • Santacruz-Toloza L., Huang Y., John S.A., Papazian D.M. Glycosylation of shaker potassium channel protein in insect cell culture and in Xenopus oocytes. Biochemistry. 33:1994;5607-5613.
    • (1994) Biochemistry , vol.33 , pp. 5607-5613
    • Santacruz-Toloza, L.1    Huang, Y.2    John, S.A.3    Papazian, D.M.4
  • 30
    • 0037194888 scopus 로고    scopus 로고
    • Conformational switch between slow and fast gating modes: Allosteric regulation of voltage sensor mobility in the EAG K+ channel
    • Schonherr R., Mannuzzu L.M., Isacoff E.Y., Heinemann S.H. Conformational switch between slow and fast gating modes. allosteric regulation of voltage sensor mobility in the EAG K+ channel Neuron. 35:2002;935-949.
    • (2002) Neuron , vol.35 , pp. 935-949
    • Schonherr, R.1    Mannuzzu, L.M.2    Isacoff, E.Y.3    Heinemann, S.H.4
  • 31
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa N.E., McCormack K., Tanouye M.A., Sigworth F.J. The size of gating charge in wild-type and mutant Shaker potassium channels. Science. 255:1992;1712-1715.
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 32
    • 0030175867 scopus 로고    scopus 로고
    • Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel
    • Seoh S.A., Sigg D., Papazian D.M., Bezanilla F. Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel. Neuron. 16:1996;1159-1167.
    • (1996) Neuron , vol.16 , pp. 1159-1167
    • Seoh, S.A.1    Sigg, D.2    Papazian, D.M.3    Bezanilla, F.4
  • 33
    • 0030896795 scopus 로고    scopus 로고
    • Topology of the Shaker potassium channel probed with hydrophilic epitope insertions
    • Shih T.M., Goldin A.L. Topology of the Shaker potassium channel probed with hydrophilic epitope insertions. J. Cell Biol. 136:1997;1037-1045.
    • (1997) J. Cell Biol. , vol.136 , pp. 1037-1045
    • Shih, T.M.1    Goldin, A.L.2
  • 34
    • 0035039731 scopus 로고    scopus 로고
    • Histidine scanning mutagenesis of basic residues of the S4 segment of the shaker K+ channel
    • Starace D.M., Bezanilla F. Histidine scanning mutagenesis of basic residues of the S4 segment of the shaker K+ channel. J. Gen. Physiol. 117:2001;469-490.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 469-490
    • Starace, D.M.1    Bezanilla, F.2
  • 36
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima C., Nomura H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature. 418:2002;605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 37
    • 0033433966 scopus 로고    scopus 로고
    • Effect of cysteine substitutions on the topology of the S4 segment of the Shaker potassium channel: Implications for molecular models of gating
    • Wang M.H., Yusaf S.P., Elliott D.J., Wray D., Sivaprasadarao A. Effect of cysteine substitutions on the topology of the S4 segment of the Shaker potassium channel. implications for molecular models of gating J. Physiol. 521:1999;315-326.
    • (1999) J. Physiol. , vol.521 , pp. 315-326
    • Wang, M.H.1    Yusaf, S.P.2    Elliott, D.J.3    Wray, D.4    Sivaprasadarao, A.5
  • 38
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White S.H., Wimley W.C. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta. 1376:1998;339-352.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 39
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • Yang N., George A.L. Jr., Horn R. Molecular basis of charge movement in voltage-gated sodium channels. Neuron. 16:1996;113-122.
    • (1996) Neuron , vol.16 , pp. 113-122
    • Yang, N.1    George, A.L.2    Horn, R.3
  • 40
    • 0029845542 scopus 로고    scopus 로고
    • Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel
    • Yusaf S.P., Wray D., Sivaprasadarao A. Measurement of the movement of the S4 segment during the activation of a voltage-gated potassium channel. Pflugers Arch. 433:1996;91-97.
    • (1996) Pflugers Arch. , vol.433 , pp. 91-97
    • Yusaf, S.P.1    Wray, D.2    Sivaprasadarao, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.