Evidence for dimerization of dimers in K+ channel assembly

Biophysical Journal

Volumn 76, Issue 4, 1999, Pages 2004-2017

  Tu, LiWei ^a   Deutsch, Carol ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; POTASSIUM CHANNEL;

ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; DIMERIZATION; FEMALE; FLUOROGRAPHY; GEL ELECTROPHORESIS; GENE EXPRESSION; GENE MUTATION; KINETICS; MOLECULAR INTERACTION; NONHUMAN; OLIGOMERIZATION; OOCYTE; PROTEIN ASSEMBLY; XENOPUS LAEVIS;

EID: 0033025560     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77358-3     Document Type: Article

References (39)

1. Babila, T., A. Moscucci, H. Wang, F. E. Weaver, and G. Korea. 1994. Assembly of mammalian voltage-gated potassium channels: evidence for an important role of the first transmembrane segment. Neuron. 12:615-626.
2. Blount, P., M. M. Smith, and J. P. Merlie. 1990. Assembly intermediates of the mouse muscle nicotinic acetylcholine receptor in stably transfected fibroblasts. J. Cell Biol. 111:2601-2611.
3. + channel are not essential for channel activity or zinc modulation. Biophys. J. 66:694-699.
4. Busch, A. E., R. S. Hurst, R. A. North, J. P. Adelman, and M. P. Kavanaugh. 1991. Current inactivation involves a histidine residue in the pore of the rat lymphocyte potassium channel RGK5. Biochem. Biophys. Res. Commun. 179:1384-1390.
5. Chahine, M., L. Chen, R. L. Barchi, R. G. Kallen, and R. Horn. 1992. Lidocaine block of human heart sodium channels expressed in Xenopus oocytes. J. Mol. Cell. Cardiol. 24:1231-1236.
6. KACh. J. Biol. Chem. 273:5271-5278.
7. + channel (SKC1): oligomeric stoichiometry and stability. Biochemistry. 36:10343-10352.
8. Deal, K. K., D. M. Lovinger, and M. M. Tamkun. 1994. The brain Kv1.1 potassium channel: in vitro and in vivo studies on subunit assembly and posttranslational processing. J. Neurosci. 14:1666-1676.
9. Doms, R. W., R. A. Lamb, J. K. Rose, and A. Helenius. 1993. Folding and assembly of viral membrane proteins. Virology. 193:545-562.
10. + conduction and selectivity. Science. 280:69-77.
11. Green, W. N., and T. Claudio. 1993. Acetylcholine receptor assembly: subunit folding and oligomerization occur sequentially. Cell. 74:57-69.
12. Gu, Y., J. R. Forsayeth, S. Verrall, X. Yu, and Z. W. Hall. 1991. Assembly of mammalian muscle acetylcholine receptors in transfected COS cells. J. Cell Biol. 114:799-807.
13. Heginbotham, L., and R. MacKinnon. 1992. The aromatic binding site for tetraethylammonium ion on potassium channels. Neuron. 8:483-491.
14. Helenius, A., T. Marquardt, and I. Braakman. 1992. The endoplasmic reticulum as a protein-folding compartment. Trends Cell Biol. 2:227-231.
15. Holsinger, L. J., and R. A. Lamb. 1991. Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology. 183:32-43.
16. + channels radically alters activation and inactivation. J. Neurosci. 17:32-44.
17. Li, M., Y. N. Jan, and L. Y. Jan. 1992. Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channels. Science. 257:1225-1230.
18. Li, M., N. Unwin, K. A. Stauffer, Y. Jan, and L. Y. Jan. 1994. Images of purified Shaker potassium channels. Curr. Biol. 4:110-114.
19. Liu, D. T., G. R. Tibbs, P. Paoletti, and S. A. Siegelbaum. 1998. Constraining ligand-binding site stoichiometry suggests that a cyclic nucleotide-gated channel is composed of two functional dimers. Neuron. 21:235-248.
20. 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.
21. MacKinnon, R. 1991. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature. 350:232-235.
22. Manolios, N., F. Letourneur, J. S. Bonifacino, and R. D. Klausner. 1991. Pairwise, cooperative and inhibitory interactions describe the assembly and probable structure of the T-cell antigen receptor. EMBO J. 10: 1643-1651.
23. + channel subunits does not ensure the stoichiometry of expressed channels. Biophys. J. 63:1406-1411.
24. Moore, W. J. 1972. Physical Chemistry, 4th Ed. Prentice Hall, Englewood Cliffs, NJ. 150.
25. Nagaya, N., and D. M. Papazian. 1997. Potassium channel a and b subunits assemble in the endoplasmic reticulum. J. Biol. Chem. 272:3022-3027.
26. Ogielska, E. M., W. N. Zagotta, T. Hoshi, S. H. Heinemann, J. Haab, and R. W. Aldrich. 1995. Cooperative subunit interactions in C-type inactivation of K channels. Biophys. J. 69:2449-2457.
27. Panyi, G., and C. Deutsch. 1996. Assembly and suppression of endogenous Kv1.3 channels in human T cells. J. Gen. Physiol. 107:409-420.
28. Panyi, G., and C. Deutsch. 1997. Anomalous inactivation of a Kv1.3 mutant. Biophys. J. 72:A27.
29. Panyi, G., Z. Sheng, L. Tu, and C. Deutsch. 1995. C-type inactivation occurs by a cooperative mechanism. Biophys. J. 69:896-904.
30. Root, M. J., and R. MacKinnon. 1994. Two identical noninteracting sites in an ion channel revealed by proton transfer. Science. 265:1852-1856.
31. Saedi, M. S., W. G. Conroy, and J. Lindstrom. 1991. Assembly of Torpedo acetylcholine receptors in Xenopus oocytes. J. Cell Biol. 112: 1007-1015.
32. Sakaguchi, T., Q. Tu, L. H. Pinto, and R. A. Lamb. 1997. The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer. Proc. Natl. Acad. Sci. USA. 94:5000-5005.
33. + channel are not linked by a disulfide bond. Biochemistry. 34:1725-1733.
34. + channels. Biochemistry. 35:12133-12140.
35. + channel assembly. Neuron. 11:67-76.
36. Sheng, Z., W. Skach, V. Santarelli, and C. Deutsch. 1997. Evidence for interaction between transmembrane segments in assembly of Kv1.3. Biochemistry. 36:15501-15513.
37. +channel DNA sequences specifically inhibit Kvl.3 and Kv3.1 expression in mouse T lymphocytes. Biophys. J. 68:147-156.
38. + channels contain multiple intersubunit association sites. J. Biol. Chem. 271:18904-18911.
39. Xu, W. Y., J. N. Jan, L. Jan, and M. Li. 1995. Assembly of voltage-gated potassium channels. Conserved hydrophilic motifs determine subfamily-specific interactions between the a-subunits. J. Biol. Chem. 270: 24761-24768.