메뉴 건너뛰기




Volumn 333, Issue 1, 2003, Pages 103-116

Structural characterisation of neuronal voltage-sensitive K+ channels heterologously expressed in Pichia pastoris

Author keywords

Channel; Electron microscopy; Expression; Structure

Indexed keywords

BACTERIAL PROTEIN; DENDROTOXIN; IODINE 125; LIPID; OLIGOMER; POTASSIUM CHANNEL; POTASSIUM ION; TETRAMER; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 0141457531     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.07.009     Document Type: Article
Times cited : (39)

References (66)
  • 2
    • 0001847927 scopus 로고    scopus 로고
    • Cloned potassium channels from eukaryotes and prokaryotes
    • Jan L.Y., Jan Y.N. Cloned potassium channels from eukaryotes and prokaryotes. Annu. Rev. Neurosci. 20:1997;91-123.
    • (1997) Annu. Rev. Neurosci. , vol.20 , pp. 91-123
    • Jan, L.Y.1    Jan, Y.N.2
  • 3
    • 0026486232 scopus 로고
    • Molecular biology of voltage-dependent potassium channels
    • Pongs O. Molecular biology of voltage-dependent potassium channels. Physiol. Rev. 72:1992;S69-S89.
    • (1992) Physiol. Rev. , vol.72
    • Pongs, O.1
  • 4
    • 0029161835 scopus 로고
    • + channels nets yet more diversity
    • + channels nets yet more diversity. Neuron. 15:1995;489-492.
    • (1995) Neuron , vol.15 , pp. 489-492
    • Salkoff, L.1    Jegla, T.2
  • 6
    • 0028841033 scopus 로고
    • A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans
    • Schrempf H., Schmidt O., Kummerlen R., Hinnah S., Müller D., Betzler M., et al. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 14:1995;5170-5178.
    • (1995) EMBO J. , vol.14 , pp. 5170-5178
    • Schrempf, H.1    Schmidt, O.2    Kummerlen, R.3    Hinnah, S.4    Müller, D.5    Betzler, M.6
  • 7
    • 0033582936 scopus 로고    scopus 로고
    • Transmembrane structure of an inwardly rectifying potassium channel
    • Minor D.L., Masseling S.J., Jan Y.N., Jan L.Y. Transmembrane structure of an inwardly rectifying potassium channel. Cell. 96:1999;879-891.
    • (1999) Cell , vol.96 , pp. 879-891
    • Minor, D.L.1    Masseling, S.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 8
    • 0024044104 scopus 로고
    • +-channel protein identified by its binding-properties for dendrotoxin-I
    • +-channel protein identified by its binding-properties for dendrotoxin-I. Proc. Natl Acad. Sci. USA. 85:1988;4919-4923.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4919-4923
    • Rehm, H.1    Lazdunski, M.2
  • 10
    • 0026457562 scopus 로고
    • Oligomeric properties of alpha-dendrotoxin-sensitive potassium-ion channels purified from bovine brain
    • Parcej D.N., Scott V.E.S., Dolly J.O. Oligomeric properties of alpha-dendrotoxin-sensitive potassium-ion channels purified from bovine brain. Biochemistry. 31:1992;11084-11088.
    • (1992) Biochemistry , vol.31 , pp. 11084-11088
    • Parcej, D.N.1    Scott, V.E.S.2    Dolly, J.O.3
  • 14
    • 0029862913 scopus 로고    scopus 로고
    • Beta-subunits promote K+ channel surface expression through effects early in biosynthesis
    • Shi G.Y., Nakahira K., Hammond S., Rhodes K.J., Schechter L.E., Trimmer J.S. Beta-subunits promote K+ channel surface expression through effects early in biosynthesis. Neuron. 16:1996;843-852.
    • (1996) Neuron , vol.16 , pp. 843-852
    • Shi, G.Y.1    Nakahira, K.2    Hammond, S.3    Rhodes, K.J.4    Schechter, L.E.5    Trimmer, J.S.6
  • 15
    • 0031020241 scopus 로고    scopus 로고
    • Potassium channel alpha and beta subunits assemble in the endoplasmic reticulum
    • Nagaya N., Papazian D.M. Potassium channel alpha and beta subunits assemble in the endoplasmic reticulum. J. Biol. Chem. 272:1997;3022-3027.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3022-3027
    • Nagaya, N.1    Papazian, D.M.2
  • 16
  • 17
    • 0032580205 scopus 로고    scopus 로고
    • Crystal-structure of the tetramerization domain of the shaker potassium channel
    • Kreusch A., Pfaffinger P.J., Stevens C.F., Choe S. Crystal-structure of the tetramerization domain of the shaker potassium channel. Nature. 392:1998;945-948.
    • (1998) Nature , vol.392 , pp. 945-948
    • Kreusch, A.1    Pfaffinger, P.J.2    Stevens, C.F.3    Choe, S.4
  • 21
    • 14444278973 scopus 로고    scopus 로고
    • Purification, visualization, and biophysical characterization of Kv1.3 tetramers
    • Spencer R.H., Sokolov Y., Li H.L., Takenaka B., Milici A.J., Aiyar J., et al. Purification, visualization, and biophysical characterization of Kv1.3 tetramers. J. Biol. Chem. 272:1997;2389-2395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2389-2395
    • Spencer, R.H.1    Sokolov, Y.2    Li, H.L.3    Takenaka, B.4    Milici, A.J.5    Aiyar, J.6
  • 23
    • 0027000070 scopus 로고
    • + channels raised using alpha-dendrotoxin acceptors purified from bovine brain
    • + channels raised using alpha-dendrotoxin acceptors purified from bovine brain. Biochemistry. 31:1992;12297-12303.
    • (1992) Biochemistry , vol.31 , pp. 12297-12303
    • Muniz, Z.M.1    Parcej, D.N.2    Dolly, J.O.3
  • 24
    • 0027146670 scopus 로고
    • Tyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled m1 muscarinic acetylcholine receptor
    • Huang X.Y., Morielli A.D., Peralta E.G. Tyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled m1 muscarinic acetylcholine receptor. Cell. 75:1993;1145-1156.
    • (1993) Cell , vol.75 , pp. 1145-1156
    • Huang, X.Y.1    Morielli, A.D.2    Peralta, E.G.3
  • 25
    • 0029026780 scopus 로고
    • Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation
    • Levin G., Keren T., Peretz T., Chikvashvili D., Thornhill W.B., Lotan I. Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation. J. Biol. Chem. 270:1995;14611-14618.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14611-14618
    • Levin, G.1    Keren, T.2    Peretz, T.3    Chikvashvili, D.4    Thornhill, W.B.5    Lotan, I.6
  • 27
    • 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
  • 28
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly P.J., Krebs E.G. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J. Biol. Chem. 266:1991;15555-15558.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 29
    • 0348003908 scopus 로고    scopus 로고
    • Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter
    • Tate C.G., Haase J., Baker C., Boorsma M., Magnani F., Vallis V., Williams D.C. Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter. Biochim. Biophys. Acta. 1610:2003;141-153.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 141-153
    • Tate, C.G.1    Haase, J.2    Baker, C.3    Boorsma, M.4    Magnani, F.5    Vallis, V.6    Williams, D.C.7
  • 32
    • 0031838466 scopus 로고    scopus 로고
    • Toxin and subunit specificity of blocking affinity of 3 peptide toxins for heteromultimeric, voltage-gated potassium channels expressed in Xenopus oocytes
    • Hopkins W.F. Toxin and subunit specificity of blocking affinity of 3 peptide toxins for heteromultimeric, voltage-gated potassium channels expressed in Xenopus oocytes. J. Pharmacol. Exptl Ther. 285:1998;1051-1060.
    • (1998) J. Pharmacol. Exptl Ther. , vol.285 , pp. 1051-1060
    • Hopkins, W.F.1
  • 33
    • 0141821904 scopus 로고    scopus 로고
    • Mapping of a dendrotoxin binding-site - Determination of toxin residues affecting affinity to romk1 potassium channel
    • Imredy J.P., Mackinnon R. Mapping of a dendrotoxin binding-site - determination of toxin residues affecting affinity to romk1 potassium channel. Biophys. J. 74:1998;86.
    • (1998) Biophys. J. , vol.74 , pp. 86
    • Imredy, J.P.1    Mackinnon, R.2
  • 34
    • 0028973231 scopus 로고
    • The alpha-dendrotoxin footprint on a mammalian potassium channel
    • Tytgat J., Debont T., Carmeliet E., Daenens P. The alpha-dendrotoxin footprint on a mammalian potassium channel. J. Biol. Chem. 270:1995;24776-24781.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24776-24781
    • Tytgat, J.1    Debont, T.2    Carmeliet, E.3    Daenens, P.4
  • 35
    • 0022545739 scopus 로고
    • Involvement of neuronal acceptors for dendrotoxin in its convulsive action in rat brain
    • Black A.R., Breeze A.L., Othman I.B., Dolly J.O. Involvement of neuronal acceptors for dendrotoxin in its convulsive action in rat brain. Biochem. J. 237:1986;397-404.
    • (1986) Biochem. J. , vol.237 , pp. 397-404
    • Black, A.R.1    Breeze, A.L.2    Othman, I.B.3    Dolly, J.O.4
  • 36
    • 0033593015 scopus 로고    scopus 로고
    • Recreation of neuronal Kv1 channel oligomers by expression in mammalian cells using Semliki Forest virus
    • Shamotienko O., Akhtar S., Sidera C., Meunier F.A., Ink B., Weir M., Dolly J.O. Recreation of neuronal Kv1 channel oligomers by expression in mammalian cells using Semliki Forest virus. Biochemistry. 38:1999;16766-16776.
    • (1999) Biochemistry , vol.38 , pp. 16766-16776
    • Shamotienko, O.1    Akhtar, S.2    Sidera, C.3    Meunier, F.A.4    Ink, B.5    Weir, M.6    Dolly, J.O.7
  • 37
    • 0024419121 scopus 로고
    • Interactions between dendrotoxin, a blocker of voltage-dependent potassium channels, and charybdotoxin, a blocker of calcium-activated potassium channels, at binding sites on neuronal membranes
    • Harvey A.L., Marshall D.L., De-Allie F.A., Strong P.N. Interactions between dendrotoxin, a blocker of voltage-dependent potassium channels, and charybdotoxin, a blocker of calcium-activated potassium channels, at binding sites on neuronal membranes. Biochem. Biophys. Res. Commun. 163:1989;394-397.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 394-397
    • Harvey, A.L.1    Marshall, D.L.2    De-Allie, F.A.3    Strong, P.N.4
  • 39
    • 0035782688 scopus 로고    scopus 로고
    • The first three-dimensional structure of phosphofructokinase from Saccharomyces cerevisiae determined by electron microscopy of single particles
    • Ruiz T., Kopperschlager G., Radermacher M. The first three-dimensional structure of phosphofructokinase from Saccharomyces cerevisiae determined by electron microscopy of single particles. J. Struct. Biol. 136:2001;167-180.
    • (2001) J. Struct. Biol. , vol.136 , pp. 167-180
    • Ruiz, T.1    Kopperschlager, G.2    Radermacher, M.3
  • 42
    • 0035078574 scopus 로고    scopus 로고
    • Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution
    • Sokolova O., Kolmakova-Partensky L., Grigorieff N. Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution. Structure. 9:2001;215-220.
    • (2001) Structure , vol.9 , pp. 215-220
    • Sokolova, O.1    Kolmakova-Partensky, L.2    Grigorieff, N.3
  • 44
    • 0028059991 scopus 로고    scopus 로고
    • Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi 29 connectors in ice
    • Valpuesta J.M., Carrascosa J.L., Henderson R. Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi 29 connectors in ice. J. Mol. Biol. 240:1999;281-287.
    • (1999) J. Mol. Biol. , vol.240 , pp. 281-287
    • Valpuesta, J.M.1    Carrascosa, J.L.2    Henderson, R.3
  • 45
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of SecYEG, the bacterial protein translocation core complex
    • Breyton C., Haase W., Rapoport T.A., Kühlbrandt W., Collinson I.R. Three-dimensional structure of SecYEG, the bacterial protein translocation core complex. Nature. 418:2002;662-665.
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kühlbrandt, W.4    Collinson, I.R.5
  • 49
    • 0029865819 scopus 로고    scopus 로고
    • Molecular interaction between the Strep tag affinity peptide and its cognate target streptavidin
    • Schmidt T.G.M., Köpke J., Frank R., Skerra A. Molecular interaction between the Strep tag affinity peptide and its cognate target streptavidin. J. Mol. Biol. 225:1996;753-776.
    • (1996) J. Mol. Biol. , vol.225 , pp. 753-776
    • Schmidt, T.G.M.1    Köpke, J.2    Frank, R.3    Skerra, A.4
  • 50
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins
    • Skerra A., Schmidt T. Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol. 326:2000;271-304.
    • (2000) Methods Enzymol. , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.2
  • 52
    • 0030061225 scopus 로고    scopus 로고
    • Phosphate glass as a phosphate source in high cell density Escherichia coli fermentations
    • Curless C., Baclaski J., Sachdev R. Phosphate glass as a phosphate source in high cell density Escherichia coli fermentations. Biotechnol. Prog. 12:1996;22-25.
    • (1996) Biotechnol. Prog. , vol.12 , pp. 22-25
    • Curless, C.1    Baclaski, J.2    Sachdev, R.3
  • 53
    • 0020562171 scopus 로고
    • A rapid filtration assay for soluble receptors using polyethylenimine-treated filters
    • Bruns R.F., Lawson-Wendling K., Pugsley T.A. A rapid filtration assay for soluble receptors using polyethylenimine-treated filters. Anal. Biochem. 132:1983;74-81.
    • (1983) Anal. Biochem. , vol.132 , pp. 74-81
    • Bruns, R.F.1    Lawson-Wendling, K.2    Pugsley, T.A.3
  • 55
    • 0025727295 scopus 로고
    • Structural studies of human alpha 2-macroglobulin: Concordance between projected views obtained by negative-stain and cryoelectron microscopy
    • Stoops J.K., Schroeter J.P., Bretaudiere J.P., Olson N.H., Baker T.S., Strickland D.K. Structural studies of human alpha 2-macroglobulin: concordance between projected views obtained by negative-stain and cryoelectron microscopy. J. Struct. Biol. 106:1991;172-178.
    • (1991) J. Struct. Biol. , vol.106 , pp. 172-178
    • Stoops, J.K.1    Schroeter, J.P.2    Bretaudiere, J.P.3    Olson, N.H.4    Baker, T.S.5    Strickland, D.K.6
  • 56
    • 0035782681 scopus 로고    scopus 로고
    • The structure of the V1-ATPase determined by three-dimensional electron microscopy of single particles
    • Radermacher M., Ruiz T., Wieczorek H., Gruber G. The structure of the V1-ATPase determined by three-dimensional electron microscopy of single particles. J. Struct. Biol. 135:2001;26-37.
    • (2001) J. Struct. Biol. , vol.135 , pp. 26-37
    • Radermacher, M.1    Ruiz, T.2    Wieczorek, H.3    Gruber, G.4
  • 58
    • 0024244421 scopus 로고
    • Studying ribosome structure by electron microscopy and computer-image processing
    • Frank J., Radermacher M., Wagenknecht T., Verschoor A. Studying ribosome structure by electron microscopy and computer-image processing. Methods Enzymol. 164:1988;3-35.
    • (1988) Methods Enzymol. , vol.164 , pp. 3-35
    • Frank, J.1    Radermacher, M.2    Wagenknecht, T.3    Verschoor, A.4
  • 59
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:1999;82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 60
    • 0028375920 scopus 로고
    • Three-dimensional reconstruction from random projections: Orientational alignment via Radon transforms
    • Radermacher M. Three-dimensional reconstruction from random projections: orientational alignment via Radon transforms. Ultramicroscopy. 53:1994;121-136.
    • (1994) Ultramicroscopy , vol.53 , pp. 121-136
    • Radermacher, M.1
  • 61
    • 0033572575 scopus 로고    scopus 로고
    • Fast and accurate three-dimensional reconstruction from projections with random orientations via Radon transforms
    • Lanzavecchia S., Bellon P.L., Radermacher M. Fast and accurate three-dimensional reconstruction from projections with random orientations via Radon transforms. J. Struct. Biol. 128:1999;152-164.
    • (1999) J. Struct. Biol. , vol.128 , pp. 152-164
    • Lanzavecchia, S.1    Bellon, P.L.2    Radermacher, M.3
  • 62
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:1996;190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 64
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 65
    • 0032540273 scopus 로고    scopus 로고
    • NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice
    • Grigorieff N. NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice. J. Mol. Biol. 277:1998;1033-1046.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 66
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.