Ion conduction pore is conserved among potassium channels

被引:270
作者
Lu, Z [1 ]
Klem, AM [1 ]
Ramu, Y [1 ]
机构
[1] Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA
关键词
D O I
10.1038/35101535
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Potassium channels, a group of specialized membrane proteins, enable K+ ions to flow selectively across cell membranes. Transmembrane K+ currents underlie electrical signalling in neurons and other excitable cells. The atomic structure of a bacterial K+ channel pore has been solved by means of X-ray crystallography. To the extent that the prokaryotic pore is representative of other K+ channels, this landmark achievement has profound implications for our general understanding of K+ channels. But serious doubts have been raised concerning whether the prokaryotic K+ channel pore does actually represent those of eukaryotes. Here we have addressed this fundamental issue by substituting the prokaryotic pore into eukaryotic voltage-gated and inward-rectifier K+ channels. The resulting chimaeras retain the respective functional hallmarks of the eukaryotic channels, which indicates that the ion conduction pore is indeed conserved among K+ channels.
引用
收藏
页码:809 / 813
页数:5
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  • [1] Contribution of the S4 segment to gating charge in the Shaker K+ channel
    Aggarwal, SK
    MacKinnon, R
    [J]. NEURON, 1996, 16 (06) : 1169 - 1177
  • [3] BOND CT, 1994, RECEPTOR CHANNEL, V2, P183
  • [4] A FAMILY OF PUTATIVE POTASSIUM CHANNEL GENES IN DROSOPHILA
    BUTLER, A
    WEI, A
    BAKER, K
    SALKOFF, L
    [J]. SCIENCE, 1989, 243 (4893) : 943 - 947
  • [5] Structural compatibility between the putative voltage sensor of voltage-gated K+ channels and the prokaryotic KcsA channel
    Caprini, M
    Ferroni, S
    Planells-Cases, R
    Rueda, J
    Rapisarda, C
    Ferrer-Montiel, A
    Montal, M
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (24) : 21070 - 21076
  • [6] Functional characterization of a potassium-selective prokaryotic glutamate receptor
    Chen, GQ
    Cui, CH
    Mayer, ML
    Gouaux, E
    [J]. NATURE, 1999, 402 (6763) : 817 - 821
  • [7] ATRIAL G-PROTEIN-ACTIVATED K+-CHANNEL - EXPRESSION CLONING AND MOLECULAR-PROPERTIES
    DASCAL, N
    SCHREIBMAYER, W
    LIM, NF
    WANG, WZ
    CHAVKIN, C
    DIMAGNO, L
    LABARCA, C
    KIEFFER, BL
    GAVERIAUXRUFF, C
    TROLLINGER, D
    LESTER, HA
    DAVIDSON, N
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (21) : 10235 - 10239
  • [8] Blocker protection in the pore of a voltage-gated K+ channel and its structural implications
    del Camino, D
    Holmgren, M
    Liu, Y
    Yellen, G
    [J]. NATURE, 2000, 403 (6767) : 321 - 325
  • [9] The structure of the potassium channel:: Molecular basis of K+ conduction and selectivity
    Doyle, DA
    Cabral, JM
    Pfuetzner, RA
    Kuo, AL
    Gulbis, JM
    Cohen, SL
    Chait, BT
    MacKinnon, R
    [J]. SCIENCE, 1998, 280 (5360) : 69 - 77
  • [10] STRONG VOLTAGE-DEPENDENT INWARD RECTIFICATION OF INWARD RECTIFIER K+ CHANNELS IS CAUSED BY INTRACELLULAR SPERMINE
    FAKLER, B
    BRANDLE, U
    GLOWATZKI, E
    WEIDEMANN, S
    ZENNER, HP
    RUPPERSBERG, JP
    [J]. CELL, 1995, 80 (01) : 149 - 154