Selectivity changes during activation of mutant Shaker potassium channels

Journal of General Physiology

Volumn 110, Issue 2, 1997, Pages 101-117

  Zheng, Jie ^a   Sigworth, Fred J ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Conserved sequence; Ion channel gating; Mutagenesis; Patch clamp; Point mutation

Indexed keywords

AMMONIA; MUTANT PROTEIN; POTASSIUM CHANNEL; POTASSIUM ION; RUBIDIUM ION;

ANIMAL CELL; ARTICLE; CELL MEMBRANE DEPOLARIZATION; CHANNEL GATING; ION CONDUCTANCE; NONHUMAN; POINT MUTATION; PROTEIN STRUCTURE; XENOPUS;

AMINO ACID SEQUENCE; AMMONIA; ANIMALS; BIOTRANSFORMATION; FEMALE; ION CHANNEL GATING; KINETICS; MICE; MICE, NEUROLOGIC MUTANTS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OOCYTES; POTASSIUM; POTASSIUM CHANNELS; RUBIDIUM; XENOPUS LAEVIS;

EID: 0030818830     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.110.2.101     Document Type: Article

References (45)

1. Bezanilla, F., and C.M. Armstrong. 1977. Inactivation of the sodium channel. I. Sodium current experiments. J. Gen. Physiol. 70:549-566.
2. + channels: II. The components of gating currents and a model of channel activation. Biophys. J. 66:1011-1021.
3. Blumenthal, E.M., and L.K. Kaczmarek. 1992. Modulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes. J. Neurosci. 12:290-296.
4. Brown, A.M. 1993. Functional bases for interpreting amino acid sequences of voltage dependent K channels. Annu. Rev. Biophys. Biomol. Struct. 22:173-198.
5. Chapman, M.L., H.M.A. VanDongen, and A.M.J. VanDongen. 1997. Activation-dependent subconductance levels in the drk1 K channel suggest a subunit basis for ion permeation and gating. Biophys. J. 72:708-719.
6. Colquhoun, D., and F.J. Sigworth. 1995. Fitting and statistical analysis of single-channel records. In Single-Channel Recording. 2nd Ed. B. Sakmann and E. Neher, editors. Plenum Press, New York. 483-588.
7. + pore. Biophys. J. 65:1235-1242.
8. + pores. Pflugers Arch. 422:354-363.
9. + channel. Neuropharmacology. 35:761-773.
10. ++ interactions. Neuron. 15:1121-1132.
11. Fergusou, W.B., O.B. McManus, and K.L. Magleby. 1993. Opening and closing transitions for BK channels often occur in two steps via sojourns through a brief lifetime subconductance state. Biophys. J. 65:702-714.
12. Fox, J.A. 1987. Ion channel subconductance states. J. Membr. Biol. 97:1-8.
13. Hanke, W., and G. Boheim. 1980. The lowest conductance state of the alamethicin pore. Biochim. Biophys. Acta. 596:456-162.
14. Heginbotham, L., and R. MacKinnon. 1992. The aromatic binding site for tetraethylammonium ion on potassium channels. Neuron. 8:483-491.
15. + channel. Biophys. J. 65:2089-2096.
16. + channels. Science (Wash. DC). 258:1152-1155.
17. + channel signature sequence. Biophys. J. 60: 1061-1067.
18. Heinemann, S.H., H. Terlau, W. Stuhmer, K. Imoto, and S. Numa. 1992. Calcium channel characteristics conferred on the sodium channel by single mutations. Nature (Lond.). 356:441-143.
19. Hille, B. 1992. Ionic Channels of Excitable Membranes. 2nd Ed. Sinauer Associates, Inc. Sunderland, MA.
20. Hoshi, T., W. N. Zagotta, and R.W. Aldrich. 1994. Shaker potassium channel gating. I: Transitions near the open state. J. Gen. Physiol. 103:249-278.
21. Kamb, A., J. Tseng-Crank, and M.A. Tauouye. 1988. Multiple products of the Drosophila Shaker gene may contribute to potassium channel diversity. Neuron. 1:421-430.
22. Kavanaugh, M.P., R.S. Hurst, J. Yakel, M.D. Varnum, J.P. Adelman, and R.A. North. 1992. Multiple subunits of a voltage-dependent potassium channel contribute to the binding site for tetraethylammonium. Neuron. 8:493-197.
23. + channels determined by an interacting pair of nonpolar amino acids. Neuron. 8:499-505.
24. Li, M., N. Unwin, K.A. Stauffer, Y.N. Jan, and L.Y. Jan. 1994 Images of purified Shaker potassium channels. Curr. Biol. 4:110-115.
25. Liu, D.T., G.R. Tibbs, and S.A. Siegelbaum. 1996. Subunit stoichiometry of cyclic nucleotide-gated channels and effects of subunit order on channel function. Neuron. 16:983-990.
26. + channel comprises part of the pore. Nature (Lond.). 367:179-182.
27. Lü, Q., and C. Miller. 1995. Silver as a probe of pore-forming residues in a potassium channel. Science (Wash. DC). 268:304-307.
28. MacKinnon, R. 1995. Pore loops: an emerging theme in ion channel structure. Neuron. 14:889-892.
29. MacKinnon, R., and C. Miller. 1989. Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor. Science (Wash. DC). 245:1382-1385.
30. + channels. Science (Wash. DC). 250:276-279.
31. + channel: evidence for a fluctuating barrier mechanism. J. Gen. Physiol. 107: 47-68.
32. + channels. Biophys. J. 66:1929-1938.
33. Schneggenburger, R., and P. Ascher. 1997. Coupling of permeation and gating in an NMDA-channel pore mutant. Neuron. 18: 167-177.
34. Schwarz, T.L., and L.Y. Jan. 1988. Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila. Nature (Lond.). 331:137-142.
35. Sigworth, F.J. 1994. Voltage gating of ion channels. Q. Rev. Biophys. 27:1-40.
36. Stühmer, W., F. Conti, M. Stocker, O. Pongs, and S.H. Heinemann. 1991. Gating currents of inactivating and non-inactivating potassium channels expressed in Xenopus oocytes. Pflugers Arch. 418: 423-429.
37. + channel with altered pore structure and function. Biophys. J. 62:34-36.
38. + pores. Pflugers Arch. 423:104-112.
39. Warmke, J.W., and B. Ganetzky. 1994. A family of potassium channel genes related to eag in Drosophila and mammals. Proc. Natl. Acad. Sci. USA. 91:3438-3442.
40. + channel. Science (Wash. DC). 251:939-942.
41. + channel by mutation of the H5 region. Nature (Lond). 349: 700-704.
42. + channel. Biophys. J. 68:448-458.
43. + channel. Biophys. J. 71:2467-2472.
44. Zagotta, W.N., T. Hoshi, J. Dittman, and R.W. Aldrich. 1994a. Shaker potassium channel gating. II: Transitions in the activation pathway. J. Gen. Physiol. 103:279-319.
45. Zagotta, W.N., T. Hoshi, and R.W. Aldrich. 1994b. Shaker potassium channel gating. III: Evaluation of kinetic models for activation. J. Gen. Physiol. 103:321-362.