Structural and functional role of the extracellular S5-P linker in the HERG potassium channel

Journal of General Physiology

Volumn 120, Issue 5, 2002, Pages 723-737

  Liu, Jie ^a   Zhang, Mei ^a   Jiang, Min ^a   Tseng, Gea Ny ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

Cysteine scanning mutagenesis; LQT2; Oocyte expression; Rapid delayed rectifier K channel

Indexed keywords

CYSTEINE; DISULFIDE; GENE PRODUCT; POTASSIUM CHANNEL; PROTEIN HERG; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL; CATION TRANSPORT PROTEIN; DITHIOTHREITOL; KCNH6 PROTEIN, HUMAN; MESYLIC ACID DERIVATIVE; POTASSIUM CHANNEL HERG;

ACTION POTENTIAL; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL FUNCTION; CELL STRUCTURE; CHANNEL GATING; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ELECTRIC POTENTIAL; EXTRACELLULAR SPACE; KINETICS; MUTAGENESIS; NONHUMAN; PHENOTYPE; POROSITY; POTASSIUM TRANSPORT; PROTEIN INTERACTION; PROTEIN STRUCTURE; SENSOR; AMINO ACID SUBSTITUTION; ANIMAL; CELL MEMBRANE POTENTIAL; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; METABOLISM; OOCYTE; PATCH CLAMP; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; XENOPUS LAEVIS;

AMINO ACID SUBSTITUTION; ANIMALS; CATION TRANSPORT PROTEINS; CYSTEINE; DITHIOTHREITOL; ETHER-A-GO-GO POTASSIUM CHANNELS; ION CHANNEL GATING; MEMBRANE POTENTIALS; MESYLATES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OOCYTES; PATCH-CLAMP TECHNIQUES; POTASSIUM CHANNELS; POTASSIUM CHANNELS, VOLTAGE-GATED; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS LAEVIS;

EID: 0036845677     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.20028687     Document Type: Article

References (36)

1. + channel. Nat. Struct. Biol. 7:309-311.
2. Cha, A., G.E. Snyder, P.R. Selvin, and F. Bezanilla. 1999. Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature 402:809-813.
3. Cornette, J.L., K.B. Cease, H. Margalit, J.L. Spouge, J.A. Berzofsky, and C. DeLisi. 1987. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195:659-685.
4. + conduction and selectivity. Science 280:69-77.
5. Dun, W., M. Jiang, and G.-N. Tseng. 1999a. Allosteric effects of mutations in the extracellular S5-P loop on the gating and ion permeation properties of hERG. Pflugers Arch. 439:141-149.
6. Dun, W., M. Jiang, S. Zeng, and G.-N. Tseng. 1999b. Differences in the effects and state-dependence of MTS modification of an outer mouth cysteine residue reveal differences between HERG and Shakerin structural rearrangements involved in C-type inactivation. Circulation 100:1842.
7. Fan, J.-S., M. Jiang, W. Dun, T.V. McDonald, and G.-N. Tseng. 1999. Effects of outer mouth mutations on hERG channel function: A comparison with similar mutations in Shaker. Biophys. J. 76:3128-3140.
8. Fedida, D., N.D. Maruoka, and S. Lin. 1999. Modulation of slow inactivation in human cardiac Kvl.5 channels by extra- and intracellular permeant cations. J. Physiol. 515:315-329.
9. + channel. Neuron 27:585-595.
10. Glauner, K.S., L.M. Mannuzzu, C.S. Gandhi, and E.Y. Isacoff. 1999. Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel. Nature 402:813-817.
11. Hancox, J.C., A.J. Levi, and H.J. Witchel. 1998. Time course and voltage dependence of expressed HERG current compared with native "rapid" delayed rectifier K current during the cardiac ventricular action potential. Pflugers Arch. 436:843-853.
12. Heginbotham, L., and R. MacKinnon. 1992. The aromatic binding site for tetraethylammonium ion on potassium channels. Neuron 8:483-491.
13. + channel pore through mutant cycles with a peptide inhibitor. Science 268:307-310.
14. + channels: Effects of alterations in the carboxy-terminal region. Neuron 7:547-556.
15. Klemic, K.G., C.-C. Shieh, G.E. Kirsch, and S.W. Jones. 1998. Inactivation of Kv2.1 potassium channels. Biophys. J. 74:1779-1789.
16. + channels. Neuron 27:573-583.
17. + channel. J. Gen. Physiol. 115:33-49.
18. + channel during gating. Neuron 16: 859-867.
19. Lopez-Barneo, J., T. Hoshi, S.H. Heinemann, and R.W. Aldrich. 1993. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels. 1:61-71.
20. + channel-blocking peptides. Neuron 15:5-10.
21. Mitcheson, J.S., J. Chen, and M.C. Sanguinetti. 2000. Trapping of a methanesulfonanilide by closure of the HERG potassium channel activation gate. J. Gen. Physiol. 115:229-239.
22. + channels. J. Gen. Physiol. 116:181-190.
23. + channel occurs by a cooperative mechanism. Biophys. J. 69:896-903.
24. Pardo-Lopez, L., M. Zhang, J. Liu, M. Jiang, L.D. Possani, and G.-N. Tseng. 2002. Mapping the binding site of a HERG-specific peptide toxin (ErgTx) to the channel's outer vestibule. J. Biol. Chem. 277:16403-16411.
25. + channel (Kv1.4) expressed in Xenopus oocytes. J. Physiol. 489:709-721.
26. + channels. Circ. Res. 82:739-750.
27. Kr potassium channel. Cell 81: 299-307.
28. Schreibmayer, W., H.A. Lester, and N. Dascal. 1994. Voltage clamping of Xenopus laevis oocytes utilizing agarose-cushion electrodes. Pflugers Arch. 426:453-458.
29. Smith, P.L., T. Baukrowitz, and G. Yellen. 1996. The inward rectification mechanism of the HERG cardiac potassium channel. Nature 379:833-836.
30. Kr channel. J. Gen. Physiol. 107:611-619.
31. Splawski, I.,J. Shen, K.W. Timothy, M.H. Lehmann, S.G. Priori, J.L. Robinson, A.J. Moss, P.J. Schwartz, J.A. Towbin, G.M. Vincent, and M.T. Keating. 2000. Spectrum of mutations in long-QT syndrome genes KvLQT1, HERG, SCN5A, KCNE1, and KCNE2. Circulation 102:1178-1185.
32. Starkus, J.G., L. Kuschel, M.D. Rayner, and S.H. Heinemann. 1997. Ion conduction through C-type inactivated Shaker channels. J. Gen. Physiol. 110:539-550.
33. Tseng-Crank, J.C.L., G.-N. Tseng, A. Schwartz, and M.A. Tanouye. 1990. Molecular cloning and functional expression of a potassium channel cDNA isolated from a rat cardiac library. FEBS Lett. 268:63-68.
34. Kr: The hERG channel. J. Mol. Cell. Cardiol. 33: 835-849.
35. + channel allows inactivation to be modulated by metal binding. Biophys. J. 66: 1068-1075.
36. Zhou, J., Q. Gong, B. Ye, Z. Fan, J.C. Makielski, G.A. Robertson, and C.T. January. 1998. Properties of HERG channels stably expressed in HEK 293 cells studied at physiological temperature. Biophys. J. 74:230-241.