Potassium channel structure: Domain by domain

Current Opinion in Structural Biology

Volumn 10, Issue 4, 2000, Pages 456-461

  Biggin, Phil C ^a   Roosild, Tarmo ^a   Choe, Senyon ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; LOCAL ANESTHETIC AGENT; MEMBRANE PROTEIN; POTASSIUM CHANNEL;

CHIMERA; DRUG TARGETING; ELECTRIC POTENTIAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; REVIEW;

EID: 0033930875     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00114-7     Document Type: Review

References (48)

1. + channels. Ann NY Acad Sci. 868:1999;233-285.
2. + conduction and selectivity. Science. 280:1998;69-77. This paper reports the first X-ray structure of an ion-selective channel. The channel, called KcsA, is a potassium channel found in the bacterium Streptomyces lividans. The channel is composed of a tetramer of subunits, each with two transmembrane helices. The ion selectivity is accomplished by a highly conserved region located near the extracellular mouth, in which backbone carbonyl oxygens line the pore.
3. Reyes R., Lauritzen I., Lesage F., Ettaiche M., Fosset M., Lazdunski M. Immunolocalization of the arachidonic acid and mechanosensitive baseline TRAAK potassium channel in the nervous system. Neuroscience. 95:2000;893-901.
4. + channels. Ann NY Acad Sci. 868:1999;286-303.
5. + channel subunit proteins. Neuron. 14:1995;625-633.
6. Xu J., Yu W., Jan Y-N., Jan L., Li M. Assembly of voltage-gated potassium channels. J Biol Chem. 270:1995;24 761-24 768.
7. Kreusch A., Pfaffinger P.J., Stevens C.F., Choe S. Crystal structure of the tetramerization domain of the Shaker potassium channel. Nature. 392:1998;945-948. The authors show that the cytoplasmic T1 domain can exist as a stable tetramer. The structure raised questions about how the ions get to the transmembrane part of the potassium channel. There is a water-filled cavity through the center of the T1 domain, but electrostatic and binding experiments suggest that ions cannot pass through it as it currently exists. Current views postulate ions passing around the T1 domain and through other parts of the protein chain, most probably between the inner leaflet of the membrane and the C-terminal side of the T1 tetramer.
8. + channels with altered functional properties. Neuron. 19:1997;711-722.
9. Aravind L., Koonin E.V. Fold prediction and evolutionary analysis of the POZ domain: structural and evolutionary relationship with the potassium channel tetramerization domain. J Mol Biol. 285:1999;1353-1361. The authors predicted the fold of the POZ domain by sequence analysis techniques. Independently, the prediction was confirmed by X-ray crystallography [10].
10. Ahmad K.F., Engel C.K., Privé G.G. Crystal structure of the BTB domain from PLZF. Proc Natl Acad Sci USA. 95:1998;12 123-12 128.
11. Stebbins C.E., Kaelin W.G., Pavletich N.P. Structure of the VHL ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science. 284:1999;455-461. This paper not only revealed, quite unexpectedly, the presence of a fold similar to that of the T1 domain, but also highlighted the fact that this fold appears to be able to employ a variety of its interfaces for protein-protein interactions.
12. Morais Cabral J.H., Lee A., Cohen S.L., Chait B.T., Li M., MacKinnon R. Crystal structure and functional analysis of the HERG potassium channel N-terminus: a eukaryotic PAS domain. Cell. 95:1998;649-655. In this paper, the authors show that the HERG potassium channel employs its N terminus as a PAS domain; this has implications for signaling.
13. Ludwig J., Owen D., Pongs O. Carboxy-terminal domain mediates assembly of the voltage-gated rat ether-a-go-go potassium channel. EMBO J. 16:1997;6337-6345.
14. Schmitt N., Schwarz M., Peretz A., Abitbol I., Attali B., Pongs O. A recessive C-terminal Jervell and Lange-Nielsen mutation of the KCNQ1 channel impairs subunit assembly. EMBO J. 19:2000;332-340.
15. Antz C., Bauer T., Kalbacher H., Frank R., Covarrubias M., Kalbitzer H.R., Ruppersberg J.P., Baukrowitz T., Fakler B. Control of channel gating by protein phosphorylation: structural switches of the inactivation gate. Nat Struct Biol. 6:1999;146-150. This paper shows how the phosphorylation of serine residues by protein kinase C is able to effect the inactivation properties of a potassium channel.
16. Cushman S.J., Nanao M.H., Jahng A.W., DeRubeis D., Choe S., Pfaffinger P.J. Voltage-dependent activation of potassium channels is coupled to T1 domain structure. Nat Struct Biol. 7:2000;403-407. This work shows an intriguing energetic link between the conformational change in T1 on the putative membrane-facing side and the shift in the channel excitability by point mutations.
17. Holmes T.C., Fadool D.A., Ren R., Levitan I.B. Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain. Science. 274:1996;2089-2091.
18. + channels involved in mediating protein-protein interactions. Biochem Biophys Res Commun. 232:1997;585-589.
19. Wickman K.D., Clapham D.E. G-protein regulation of ion channels. Curr Opin Neurobiol. 5:1995;278-285.
20. Kornau H-C., Seeburg P.H., Kennedy M.B. Interaction of ion channels and receptors with PDZ domains. Curr Opin Neurobiol. 7:1997;368-373.
21. + channel β subunits. Ann NY Acad Sci. 868:1999;344-355.
22. + channels altered by presence of β-subunit. Nature. 369:1994;289-294.
23. Nagaya N., Papazian D.M. Potassium channel alpha and beta subunits assemble in the endoplasmic reticulum. J Biol Chem. 272:1997;3022-3027.
24. + channel surface expression through effects early in biosynthesis. Neuron. 16:1996;843-852.
25. + channel β subunit. Cell. 97:1999;943-952. This paper shows that the structure of the β subunit of potassium channels is based upon that of an aldo-keto reductase. Although little is known about the orientation of this tetramer with respect to the other potassium channel domains, the authors make a reasonable argument as to how this domain could directly regulate the channel activity of the α subunit and thus show how channel activity can be directly linked to the chemistry of the cell.
26. Chouinard S.W., Wilson G.F., Schlimgen A.K., Ganetzky B. A potassium channel beta subunit related to the aldo-keto reductase superfamily is encoded by the Drosophila hyperkinetic locus. Proc Natl Acad Sci USA. 92:1995;6763-6767.
27. Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A. An unlikely sugar substrate site in the 1.65 Å structure of the human aldose-reductase holoenzyme implicated in diabetic complications. Science. 257:1992;81-84.
28. Levitan I. Modulation of ion channels by protein phosphorylation and dephosphorylation. Ann Rev Physiol. 56:1994;193-212.
29. + channels. Nat Neurosci. 2:1999;422-426. This work nicely shows how the two-pore-domain family of potassium channels is likely to be a target of anesthetics. The two-pore-domain family is a relatively recent discovery, but it is increasingly clear that it may play very important roles throughout cellular systems.
30. + channels. Biophys J. 78:2000;2035.
31. MacKinnon R., Cohen S.L., Kuo A., Lee A., Chait B.T. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 280:1998;106-109. The authors show, using toxin-binding experiments, that the pore structure of eukaryotic potassium channels is likely to be similar to that of prokaryotes, thus highlighting the premise that bacterial systems are good enough representations of their higher organism counterparts.
32. Chen G., Cui C., Mayer M.L., Gouaux E. Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature. 402:1999;817-821. The authors show that glutamate receptors do, in fact, exist in prokaryotes, something not generally believed before now. Furthermore, the work has important consequences for the evolution of ion channels. The receptor studied here is potassium-selective and, remarkably, upon closer inspection, reveals sequence similarities to the KcsA potassium channel. It seems probable that the potassium selectivity of both proteins is strongly related in evolutionary terms.
33. + in bacterial transport. Mol Microbiol. 9:1993;533-543.
34. An W.F., Bowley M.R., Betty M., Cao J., Ling H.P., Mendoza G., Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J. Modulation of A-type potassium channels by a family of calcium sensors. Nature. 403:2000;553-556. This work demonstrates directly a new role of T1 in mediating intracellular calcium signals to neuronal excitability through protein-protein interaction with T1.
35. 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. Nature. 402:1999;809-813.
36. Glauner K.S., Mannuzzu L.M., Gandhi C.S., Isacoff E.Y. Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel. Nature. 402:1999;813-817.
37. + channel activation gating. Science. 285:1999;73-77.
38. Cooper E.C., Jan L.Y. Ion channel genes and human neurological disease: recent progress, prospects and challenges. Proc Natl Acad Sci USA. 96:1999;4759-4766.
39. Schrempf H., Schmidt O., Kummerlen R., Hinnah S., Muller D., Betzler M., Steinkamp T., Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 14:1995;5170-5178.
40. + channels. Nat Struct Biol. 6:1999;38-43.
41. Roeper J., Sewing S., Zhang Y., Sommer T., Wanner S.G., Pongs O. NIP domain prevents N-type inactivation in voltage-gated potassium channels. Nature. 391:1998;390-393.
42. Antz C., Geyer M., Fakler B., Schott M.K., Guy H.R., Frank R., Ruppersberg J.P., Kalbitzer H.R. NMR structure of inactivation gates from mammalian voltage-dependent potassium channels. Nature. 385:1997;272-275.
43. + channel. J Cell Biol. 135:1996;1619-1632.
44. + channels by interaction with a family of membrane associated guanylate kinases. Nature. 378:1995;85-88.
45. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
46. Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
47. POV-Ray - the Persistence of Vision Raytracer on World Wide Web URL http://www.povray.org .
48. Gulbis, J.M., Zhou, M., Mann, S., MacKinnon, R. Structure of the cytoplasmic beta subunit - T1 assembly of voltage-dependent K channels. Science 2000, in press. This paper describes the structure of the T1-Kvβ complex, in which two tetramers are coaxially aligned so that the flat side of Kvβ faces T1 and the C-terminal side of T1 most likely faces the membrane.