Hodgkin, A. L. & Huxley, A. F. Currents carried by sodium and potassium ions through the membrane of the giant axon of Loligo. J. Physiol.116, 449–472 (1952). ArticleCASPubMedPubMed Central Google Scholar
Hodgkin, A. L. & Huxley, A. F. The dual effect of membrane potential on sodium conductance in the giant axon of Loligo. J. Physiol.116, 497–506 (1952). ArticleCASPubMedPubMed Central Google Scholar
Hodgkin, A. L. & Huxley, A. F. A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol.117, 500–544 (1952). ArticleCASPubMedPubMed Central Google Scholar
Papazian, D. M., Schwarz, T. L., Tempel, B. L., Jan, Y. N. & Jan, L. Y. Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila. Science237, 749–753 (1987). ArticleCASPubMed Google Scholar
Timpe, L. C. et al. Expression of functional potassium channels from Shaker cDNA in Xenopus oocytes. Nature331, 143–145 (1988). ArticleCASPubMed Google Scholar
Zagotta, W. N., Hoshi, T. & Aldrich, R. W. Shaker potassium channel gating. III: Evaluation of kinetic models for activation. J. Gen. Physiol.103, 321–362 (1994). ArticleCASPubMed Google Scholar
Zagotta, W. N., Hoshi, T., Dittman, J. & Aldrich, R. W. Shaker potassium channel gating. II: Transitions in the activation pathway. J. Gen. Physiol.103, 279–319 (1994). ArticleCASPubMed Google Scholar
Hoshi, T., Zagotta, W. N. & Aldrich, R. W. Shaker potassium channel gating. I: Transitions near the open state. J. Gen. Physiol.103, 249–278 (1994). ArticleCASPubMed Google Scholar
Schoppa, N. E. & Sigworth, F. J. Activation of Shaker potassium channels. III. An activation gating model for wild-type and V2 mutant channels. J. Gen. Physiol.111, 313–342 (1998). ArticleCASPubMedPubMed Central Google Scholar
Schoppa, N. E. & Sigworth, F. J. Activation of Shaker potassium channels. II. Kinetics of the V2 mutant channel. J. Gen. Physiol.111, 295–311 (1998). ArticleCASPubMedPubMed Central Google Scholar
Schoppa, N. E. & Sigworth, F. J. Activation of Shaker potassium channels. I. Characterization of voltage-dependent transitions. J. Gen. Physiol.111, 271–294 (1998). ArticleCASPubMedPubMed Central Google Scholar
Islas, L. D. & Sigworth, F. J. Voltage sensitivity and gating charge in Shaker and Shab family potassium channels. J. Gen. Physiol.114, 723–741 (1999). ArticleCASPubMedPubMed Central Google Scholar
Soler-Llavina, G. J., Holmgren, M. & Swartz, K. J. Defining the conductance of the closed state in a voltage-gated K+ channel. Neuron38, 61–67 (2003). ArticleCASPubMed Google Scholar
Doyle, D. A. et al. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science280, 69–77 (1998). The first X-ray structure of a potassium channel. The KcsA potassium channel is a prokaryotic channel fromStreptomyces lividansthat was crystallized in a closed conformation. ArticleCASPubMed Google Scholar
Zhou, Y., Morais-Cabral, J. H., Kaufman, A. & MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution. Nature414, 43–48 (2001). ArticleCASPubMed Google Scholar
Zhou, M., Morais-Cabral, J. H., Mann, S. & MacKinnon, R. Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature411, 657–661 (2001). ArticleCASPubMed Google Scholar
Jiang, Y. et al. Crystal structure and mechanism of a calcium-gated potassium channel. Nature417, 515–522 (2002). The first X-ray structure of a potassium channel in the open conformation. This paper also shows the octameric arrangement of the RCK domains that form a gating ring on the intracellular side of the channel. A detailed discussion of gating motions is presented in the companion paper, reference 60. ArticleCASPubMed Google Scholar
Kuo, A. et al. Crystal structure of the potassium channel KirBac1.1 in the closed state. Science300, 1922–1926 (2003). ArticleCASPubMed Google Scholar
Jiang, Y. et al. X-ray structure of a voltage-dependent K+ channel. Nature423, 33–41 (2003). The first X-ray structure of a voltage-activated potassium channel. This paper reports two structures for KvAP — one for the intact channel protein and another for the isolated S1–S4 voltage-sensing domain. ArticleCASPubMed Google Scholar
Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T. & MacKinnon, R. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature415, 287–294 (2002). ArticleCASPubMed Google Scholar
Koishi, R. et al. A superfamily of voltage-gated sodium channels in bacteria. J. Biol. Chem.279, 9532–9538 (2004). ArticleCASPubMed Google Scholar
Noda, M. et al. Expression of functional sodium channels from cloned cDNA. Nature322, 826–828 (1986). ArticleCASPubMed Google Scholar
Noda, M. et al. Existence of distinct sodium channel messenger RNAs in rat brain. Nature320, 188–192 (1986). ArticleCASPubMed Google Scholar
Tanabe, T. et al. Primary structure of the receptor for calcium channel blockers from skeletal muscle. Nature328, 313–318 (1987). ArticleCASPubMed Google Scholar
Goulding, E. H. et al. Molecular cloning and single-channel properties of the cyclic nucleotide-gated channel from catfish olfactory neurons. Neuron8, 45–58 (1992). ArticleCASPubMed Google Scholar
Santoro, B. et al. Identification of a gene encoding a hyperpolarization-activated pacemaker channel of brain. Cell93, 717–729 (1998). ArticleCASPubMed Google Scholar
Butler, A., Tsunoda, S., McCobb, D. P., Wei, A. & Salkoff, L. mSlo, a complex mouse gene encoding 'maxi' calcium-activated potassium channels. Science261, 221–224 (1993). ArticleCASPubMed Google Scholar
Kubo, Y., Reuveny, E., Slesinger, P. A., Jan, Y. N. & Jan, L. Y. Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel. Nature364, 802–806 (1993). ArticleCASPubMed Google Scholar
Kubo, Y., Baldwin, T. J., Jan, Y. N. & Jan, L. Y. Primary structure and functional expression of a mouse inward rectifier potassium channel. Nature362, 127–133 (1993). ArticleCASPubMed Google Scholar
Ho, K. et al. Cloning and expression of an inwardly rectifying ATP-regulated potassium channel. Nature362, 31–38 (1993). ArticleCASPubMed Google Scholar
Ketchum, K. A., Joiner, W. J., Sellers, A. J., Kaczmarek, L. K. & Goldstein, S. A. A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem. Nature376, 690–695 (1995). ArticleCASPubMed Google Scholar
Goldstein, S. A., Bockenhauer, D., O'Kelly, I. & Zilberberg, N. Potassium leak channels and the KCNK family of two-P-domain subunits. Nature Rev. Neurosci.2, 175–184 (2001). ArticleCAS Google Scholar
Chen, G. Q., Cui, C., Mayer, M. L. & Gouaux, E. Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature402, 817–821 (1999). ArticleCASPubMed Google Scholar
MacKinnon, R. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature350, 232–235 (1991). ArticleCASPubMed Google Scholar
Liman, E. R., Tytgat, J. & Hess, P. Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs. Neuron9, 861–871 (1992). ArticleCASPubMed Google Scholar
Hoshi, T., Zagotta, W. N. & Aldrich, R. W. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science250, 533–538 (1990). ArticleCASPubMed Google Scholar
Zagotta, W. N., Hoshi, T. & Aldrich, R. W. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science250, 568–571 (1990). ArticleCASPubMed Google Scholar
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. Biochemistry33, 5607–5613 (1994). ArticleCASPubMed Google Scholar
Holmgren, M., Jurman, M. E. & Yellen, G. N-type inactivation and the S4-S5 region of the Shaker K+ channel. J. Gen. Physiol.108, 195–206 (1996). ArticleCASPubMed Google Scholar
Li-Smerin, Y. & Swartz, K. J. Localization and molecular determinants of the hanatoxin receptors on the voltage-sensing domain of a K+ channel. J. Gen. Physiol.115, 673–684 (2000). ArticleCASPubMedPubMed Central Google Scholar
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, 205–218 (2001). ArticleCASPubMedPubMed Central Google Scholar
Lee, H. C., Wang, J. M. & Swartz, K. J. Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels. Neuron40, 527–536 (2003). This paper investigates the effects of a protein toxin from tarantula venom on gating charge movement, which provides evidence for a relatively extracellular position for the S3b helix when the voltage sensors are in their resting conformations. ArticleCASPubMed Google Scholar
Yang, N., George, A. L., Jr & Horn, R. Molecular basis of charge movement in voltage-gated sodium channels. Neuron16, 113–122 (1996). ArticlePubMed Google Scholar
Larsson, H. P., Baker, O. S., Dhillon, D. S. & Isacoff, E. Y. Transmembrane movement of the Shaker K+ channel S4. Neuron16, 387–397 (1996). ArticleCASPubMed Google Scholar
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, 91–97 (1996). ArticleCASPubMed Google Scholar
MacKinnon, R. & Miller, C. Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel. J. Gen. Physiol.91, 335–349 (1988). ArticleCASPubMed Google Scholar
MacKinnon, R., Heginbotham, L. & Abramson, T. Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor. Neuron5, 767–771 (1990). ArticleCASPubMed Google Scholar
Armstrong, C. M. Inactivation of the potassium conductance and related phenomena caused by quaternary ammonium ion injection in squid axons. J. Gen. Physiol.54, 553–575 (1969). ArticleCASPubMedPubMed Central Google Scholar
Armstrong, C. M. Interaction of tetraethylammonium ion derivatives with the potassium channels of giant axons. J. Gen. Physiol.58, 413–437 (1971). ArticleCASPubMedPubMed Central Google Scholar
Armstrong, C. M. Ionic pores, gates, and gating currents. Q. Rev. Biophys.7, 179–210 (1974). An intelligent review that lays out a conceptual framework for understanding the mechanisms that underlie voltage-dependent gating and cation selectivity. This review was years ahead of its time and is a true classic in the field. ArticleCASPubMed Google Scholar
Holmgren, M., Smith, P. L. & Yellen, G. Trapping of organic blockers by closing of voltage-dependent K+ channels: evidence for a trap door mechanism of activation gating. J. Gen. Physiol.109, 527–535 (1997). This paper clearly shows the trapping of quaternary ammonium compounds in the intracellular pore of the Shaker potassium channel. ArticleCASPubMedPubMed Central Google Scholar
Liu, Y., Holmgren, M., Jurman, M. E. & Yellen, G. Gated access to the pore of a voltage-dependent K+ channel. Neuron19, 175–184 (1997). A classic paper that shows the gated access of MTS reagents for Cys residues substituted in the intracellular region of the S6 segment in the Shaker potassium channel. ArticlePubMed Google Scholar
del Camino, D. & Yellen, G. Tight steric closure at the intracellular activation gate of a voltage-gated K+ channel. Neuron32, 649–656 (2001). ArticleCASPubMed Google Scholar
Holmgren, M., Shin, K. S. & Yellen, G. The activation gate of a voltage-gated K+ channel can be trapped in the open state by an intersubunit metal bridge. Neuron21, 617–621 (1998). ArticleCASPubMed Google Scholar
Kitaguchi, T., Sukhareva, M. & Swartz, K. J. Stabilizing the closed S6 gate in the Shaker Kv channel through modification of a hydrophobic seal. J. Gen. Physiol.124, 319–332 (2004). ArticleCASPubMedPubMed Central Google Scholar
Roux, B., Berneche, S. & Im, W. Ion channels, permeation, and electrostatics: insight into the function of KcsA. Biochemistry39, 13295–13306 (2000). ArticleCASPubMed Google Scholar
Jiang, Y. et al. The open pore conformation of potassium channels. Nature417, 523–526 (2002). ArticleCASPubMed Google Scholar
Perozo, E., Cortes, D. M. & Cuello, L. G. Structural rearrangements underlying K+-channel activation gating. Science285, 73–78 (1999). ArticleCASPubMed Google Scholar
Liu, Y. S., Sompornpisut, P. & Perozo, E. Structure of the KcsA channel intracellular gate in the open state. Nature Struct. Biol.8, 883–887 (2001). ArticleCASPubMed Google Scholar
Kelly, B. L. & Gross, A. Potassium channel gating observed with site-directed mass tagging. Nature Struct. Biol.10, 280–284 (2003). ArticleCASPubMed Google Scholar
Irizarry, S. N., Kutluay, E., Drews, G., Hart, S. J. & Heginbotham, L. Opening the KcsA K+ channel: tryptophan scanning and complementation analysis lead to mutants with altered gating. Biochemistry41, 13653–13662 (2002). ArticleCASPubMed Google Scholar
MacArthur, M. W. & Thornton, J. M. Influence of proline residues on protein conformation. J. Mol. Biol.218, 397–412 (1991). ArticleCASPubMed Google Scholar
Del Camino, D., Holmgren, M., Liu, Y. & Yellen, G. Blocker protection in the pore of a voltage-gated K+ channel and its structural implications. Nature403, 321–325 (2000). ArticleCASPubMed Google Scholar
Webster, S. M., Del Camino, D., Dekker, J. P. & Yellen, G. Intracellular gate opening in Shaker K+ channels defined by high-affinity metal bridges. Nature428, 864–868 (2004). This paper investigates metal bridges in the gate region of the Shaker potassium channel that are not compatible with the X-ray structures of either KcsA, which was crystallized in a closed conformation, or MthK, which was crystallized in an open conformation. ArticleCASPubMed Google Scholar
Armstrong, C. M. & Bezanilla, F. Currents related to movement of the gating particles of the sodium channels. Nature242, 459–461 (1973). ArticleCASPubMed Google Scholar
Armstrong, C. M. & Bezanilla, F. Charge movement associated with the opening and closing of the activation gates of the Na channels. J. Gen. Physiol.63, 533–552 (1974). ArticleCASPubMedPubMed Central Google Scholar
Keynes, R. D. & Rojas, E. Kinetics and steady-state properties of the charged system controlling sodium conductance in the squid giant axon. J. Physiol.239, 393–434 (1974). ArticleCASPubMedPubMed Central Google Scholar
Schneider, M. F. & Chandler, W. K. Voltage dependent charge movement of skeletal muscle: a possible step in excitation-contraction coupling. Nature242, 244–246 (1973). ArticleCASPubMed Google Scholar
Chandler, W. K., Schneider, M. F., Rakowski, R. F. & Adrian, R. H. Charge movements in skeletal muscle. Phil. Trans. R. Soc. Lond. B270, 501–505 (1975). ArticleCAS Google Scholar
Schoppa, N. E., McCormack, K., Tanouye, M. A. & Sigworth, F. J. The size of gating charge in wild-type and mutant Shaker potassium channels. Science255, 1712–1715 (1992). ArticleCASPubMed Google Scholar
Aggarwal, S. K. & MacKinnon, R. Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron16, 1169–1177 (1996). ArticleCASPubMed Google Scholar
Seoh, S. A., Sigg, D., Papazian, D. M. & Bezanilla, F. Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel. Neuron16, 1159–1167 (1996). ArticleCASPubMed Google Scholar
Noceti, F. et al. Effective gating charges per channel in voltage-dependent K+ and Ca2+ channels. J. Gen. Physiol.108, 143–155 (1996). ArticleCASPubMed Google Scholar
Hirschberg, B., Rovner, A., Lieberman, M. & Patlak, J. Transfer of twelve charges is needed to open skeletal muscle Na+ channels. J. Gen. Physiol.106, 1053–1068 (1995). ArticleCASPubMed Google Scholar
Auld, V. J. et al. A neutral amino acid change in segment IIS4 dramatically alters the gating properties of the voltage-dependent sodium channel. Proc. Natl Acad. Sci. USA87, 323–327 (1990). ArticleCASPubMedPubMed Central Google Scholar
Papazian, D. M., Timpe, L. C., Jan, Y. N. & Jan, L. Y. Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence. Nature349, 305–310 (1991). ArticleCASPubMed Google Scholar
Liman, E. R., Hess, P., Weaver, F. & Koren, G. Voltage-sensing residues in the S4 region of a mammalian K+ channel. Nature353, 752–756 (1991). ArticleCASPubMed Google Scholar
Smith-Maxwell, C. J., Ledwell, J. L. & Aldrich, R. W. Uncharged S4 residues and cooperativity in voltage-dependent potassium channel activation. J. Gen. Physiol.111, 421–439 (1998). ArticleCASPubMedPubMed Central Google Scholar
Smith-Maxwell, C. J., Ledwell, J. L. & Aldrich, R. W. Role of the S4 in cooperativity of voltage-dependent potassium channel activation. J. Gen. Physiol.111, 399–420 (1998). ArticleCASPubMedPubMed Central Google Scholar
Ledwell, J. L. & Aldrich, R. W. Mutations in the S4 region isolate the final voltage-dependent cooperative step in potassium channel activation. J. Gen. Physiol.113, 389–414 (1999). ArticleCASPubMedPubMed Central Google Scholar
Perozo, E., Santacruz-Toloza, L., Stefani, E., Bezanilla, F. & Papazian, D. M. S4 mutations alter gating currents of Shaker K channels. Biophys. J.66, 345–354 (1994). ArticleCASPubMedPubMed Central Google Scholar
Ahern, C. A. & Horn, R. Specificity of charge-carrying residues in the voltage sensor of potassium channels. J. Gen. Physiol.123, 205–216 (2004). A recent paper that examines where in S4 the addition of charged MTS moieties contributes to the total gating charge per channel. The results indicate that only the positions that are charged in the wild-type channel are capable of contributing to gating charge. ArticleCASPubMedPubMed Central Google Scholar
Yang, N. & Horn, R. Evidence for voltage-dependent S4 movement in sodium channels. Neuron15, 213–218 (1995). A classic study that investigated the movements of S4 by measuring the voltage-dependence of the reaction between MTS reagents and Cys residues substituted in S4. ArticleCASPubMed Google Scholar
Starace, D. M., Stefani, E. & Bezanilla, F. Voltage-dependent proton transport by the voltage sensor of the Shaker K+ channel. Neuron19, 1319–1327 (1997). ArticleCASPubMed Google Scholar
Starace, D. M. & Bezanilla, F. Histidine scanning mutagenesis of basic residues of the S4 segment of the Shaker K+ channel. J. Gen. Physiol.117, 469–490 (2001). ArticleCASPubMedPubMed Central Google Scholar
Mannuzzu, L. M., Moronne, M. M. & Isacoff, E. Y. Direct physical measure of conformational rearrangement underlying potassium channel gating. Science271, 213–216 (1996). This was the first study that investigated S4 movements using fluorescence spectroscopy. ArticleCASPubMed Google Scholar
Cha, A. & Bezanilla, F. Characterizing voltage-dependent conformational changes in the Shaker K+ channel with fluorescence. Neuron19, 1127–1140 (1997). ArticleCASPubMed Google Scholar
Cha, A. & Bezanilla, F. Structural implications of fluorescence quenching in the Shaker K+ channel. J. Gen. Physiol.112, 391–408 (1998). ArticleCASPubMedPubMed Central Google Scholar
Glauner, K. S., Mannuzzu, L. M., Gandhi, C. S. & Isacoff, E. Y. Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel. Nature402, 813–817 (1999). ArticleCASPubMed Google Scholar
Cha, A., Snyder, G. E., Selvin, P. R. & Bezanilla, F. Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature402, 809–813 (1999). ArticleCASPubMed Google Scholar
Gandhi, C. S., Loots, E. & Isacoff, E. Y. Reconstructing voltage sensor-pore interaction from a fluorescence scan of a voltage-gated K+ channel. Neuron27, 585–595 (2000). ArticleCASPubMed Google Scholar
Papazian, D. M. et al. Electrostatic interactions of S4 voltage sensor in Shaker K+ channel. Neuron14, 1293–1301 (1995). ArticleCASPubMed Google Scholar
Planells-Cases, R., Ferrer-Montiel, A. V., Patten, C. D. & Montal, M. Mutation of conserved negatively charged residues in the S2 and S3 transmembrane segments of a mammalian K+ channel selectively modulates channel gating. Proc. Natl Acad. Sci. USA92, 9422–9426 (1995). ArticleCASPubMedPubMed Central Google Scholar
Tiwari-Woodruff, S. K., Schulteis, C. T., Mock, A. F. & Papazian, D. M. Electrostatic interactions between transmembrane segments mediate folding of Shaker K+ channel subunits. Biophys. J.72, 1489–1500 (1997). ArticleCASPubMedPubMed Central Google Scholar
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, 33–50 (2000). ArticleCASPubMedPubMed Central Google Scholar
Starace, D. M. & Bezanilla, F. A proton pore in a potassium channel voltage sensor reveals a focused electric field. Nature427, 548–553 (2004). This paper shows the creation of a proton-conducting pore within the voltage-sensor of the Shaker potassium channel. ArticleCASPubMed Google Scholar
Bezanilla, F. Voltage sensor movements. J. Gen. Physiol.120, 465–473 (2002). An excellent review of what is known about how S4 moves during gating in voltage-activated channels. ArticleCASPubMedPubMed Central Google Scholar
Laine, M. et al. Atomic proximity between S4 segment and pore domain in Shaker potassium channels. Neuron39, 467–481 (2003). A rigorous demonstration of disulphide and metal bridge formation between residues in the N terminus of S4 and the C terminus of S5. ArticleCASPubMed Google Scholar
Laine, M., Papazian, D. M. & Roux, B. Critical assessment of a proposed model of Shaker. FEBS Lett.564, 257–263 (2004). ArticleCASPubMed Google Scholar
Gandhi, C. S., Clark, E., Loots, E., Pralle, A. & Isacoff, E. Y. The orientation and molecular movement of a K+ channel voltage-sensing domain. Neuron40, 515–525 (2003). ArticleCASPubMed Google Scholar
Broomand, A., Mannikko, R., Larsson, H. P. & Elinder, F. Molecular movement of the voltage sensor in a K+ channel. J. Gen. Physiol.122, 741–748 (2003). ArticleCASPubMedPubMed Central Google Scholar
Ahern, C. A. & Horn, R. Stirring up controversy with a voltage sensor paddle. Trends Neurosci.27, 303–307 (2004). ArticleCASPubMed Google Scholar
Cohen, B. E., Grabe, M. & Jan, L. Y. Answers and questions from the KvAP structures. Neuron39, 395–400 (2003). ArticleCASPubMed Google Scholar
Ruta, V., Jiang, Y., Lee, A., Chen, J. & MacKinnon, R. Functional analysis of an archaebacterial voltage-dependent K+ channel. Nature422, 180–185 (2003). ArticleCASPubMed Google Scholar
Swartz, K. J. & MacKinnon, R. Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites. Neuron18, 665–673 (1997). ArticleCASPubMed Google Scholar
Swartz, K. J. & MacKinnon, R. Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels. Neuron18, 675–682 (1997). ArticleCASPubMed Google Scholar
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, 415–423 (1999). ArticleCASPubMedPubMed Central Google Scholar
Tu, L., Wang, J., Helm, A., Skach, W. R. & Deutsch, C. Transmembrane biogenesis of Kv1.3. Biochemistry39, 824–836 (2000). ArticleCASPubMed Google Scholar
Cornette, J. L. et al. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol.195, 659–685 (1987). ArticleCASPubMed Google Scholar
Rees, D. C., DeAntonio, L. & Eisenberg, D. Hydrophobic organization of membrane proteins. Science245, 510–513 (1989). ArticleCASPubMed Google Scholar
Li, J., Shi, L. & Karlin, A. A photochemical approach to the lipid accessibility of engineered cysteinyl residues. Proc. Natl Acad. Sci. USA100, 886–891 (2003). ArticleCASPubMedPubMed Central Google Scholar
Karlin, A. & Akabas, M. H. Substituted-cysteine accessibility method. Methods Enzymol.293, 123–145 (1998). ArticleCASPubMed Google Scholar
Jiang, Y., Ruta, V., Chen, J., Lee, A. & MacKinnon, R. The principle of gating charge movement in a voltage-dependent K+ channel. Nature423, 42–48 (2003). This study probes the movement of the voltage-sensor paddle motif in KvAP by biotinylating specific sites and assaying for reaction with avidin, added to either external or internal solutions. The authors propose a new paddle model for voltage-sensing in which the paddle motif undergoes a relatively large membrane translocating movement during gating. ArticleCASPubMed Google Scholar
Carter, A., Ketty, V. & Blaustein, R. O. State-dependent reactivity of cysteines substituted into Shaker's gating module. Biophys. J.86, 192 (2004). Google Scholar
Lee, S. Y. & MacKinnon, R. A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom. Nature430, 232–235 (2004). ArticleCASPubMed Google Scholar
Takahashi, H. et al. Solution structure of hanatoxin1, a gating modifier of voltage-dependent K+ channels: common surface features of gating modifier toxins. J. Mol. Biol.297, 771–780 (2000). ArticleCASPubMed Google Scholar
Wang, J. M. et al. Molecular surface of tarantula toxins interacting with voltage sensors in Kv channels. J. Gen. Physiol.123, 455–467 (2004). ArticleCASPubMedPubMed Central Google Scholar
Neale, E. J., Elliott, D. J., Hunter, M. & Sivaprasadarao, A. Evidence for intersubunit interactions between S4 and S5 transmembrane segments of the Shaker potassium channel. J. Biol. Chem.278, 29079–29085 (2003). ArticleCASPubMed Google Scholar
Jiang, Q. X., Wang, D. N. & MacKinnon, R. Electron microscopic analysis of KvAP voltage-dependent K+ channels in an open conformation. Nature430, 806–810 (2004). ArticleCASPubMed Google Scholar
Senzel, L., Huynh, P. D., Jakes, K. S., Collier, R. J. & Finkelstein, A. The diphtheria toxin channel-forming T domain translocates its own NH2-terminal region across planar bilayers. J. Gen. Physiol.112, 317–324 (1998). ArticleCASPubMedPubMed Central Google Scholar
Slatin, S. L., Qiu, X. Q., Jakes, K. S. & Finkelstein, A. Identification of a translocated protein segment in a voltage-dependent channel. Nature371, 158–161 (1994). ArticleCASPubMed Google Scholar
Oh, K. J., Senzel, L., Collier, R. J. & Finkelstein, A. Translocation of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain. Proc. Natl Acad. Sci. USA96, 8467–8470 (1999). ArticleCASPubMedPubMed Central Google Scholar
Bass, R. B. et al. The structures of BtuCD and MscS and their implications for transporter and channel function. FEBS Lett.555, 111–115 (2003). ArticleCASPubMed Google Scholar
Bass, R. B., Strop, P., Barclay, M. & Rees, D. C. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science298, 1582–1587 (2002). ArticleCASPubMed Google Scholar
Fersht, A. Structure and Mechanism in Protein Science: a Guide to Enzyme Catalysis and Protein Folding 336–337 (W. H. Freeman, New York, 1999). Google Scholar
Lakowicz, J. R. Principles of Fluorescence Spectroscopy (Kluwer Academic/Plenum, New York, 1999). Book Google Scholar
Blunck, R., Starace, D. M., Correa, A. M. & Bezanilla, F. Detecting rearrangements of Shaker and NaChBac in real-time with fluorescence spectroscopy in patch-clamped mammalian cells. Biophys. J.86, 3966–3980 (2004). ArticleCASPubMedPubMed Central Google Scholar
Durell, S. R., Hao, Y. & Guy, H. R. Structural models of the transmembrane region of voltage-gated and other K+ channels in open, closed, and inactivated conformations. J. Struct. Biol.121, 263–284 (1998). ArticleCASPubMed Google Scholar
Blaustein, R. O., Cole, P. A., Williams, C. & Miller, C. Tethered blockers as molecular 'tape measures' for a voltage-gated K+ channel. Nature Struct. Biol.7, 309–311 (2000). ArticleCASPubMed Google Scholar
Cuello, L., Cortes, D. M. & Perozo, E. Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer. Science306, 491–495 (2004). A timely EPR study investigating the mobility and environmental exposure (water vs lipid) of spin labels attached to specific positions throughout S1–S4. ArticleCASPubMed Google Scholar
Gutberlet, T. & Katsaras, J. Lipid Bilayers: Structure and Interactions (Springer, Berlin; New York, 2001). Google Scholar
Perozo, E., MacKinnon, R., Bezanilla, F. & Stefani, E. Gating currents from a nonconducting mutant reveal open-closed conformations in Shaker K+ channels. Neuron11, 353–358 (1993). ArticleCASPubMed Google Scholar
Kyte, J. & Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol.157, 105–132 (1982). ArticleCASPubMed Google Scholar