Function and structure in glycine receptors and some of their relatives

Trends in Neurosciences

Volumn 27, Issue 6, 2004, Pages 337-344

  Colquhoun, David ^a   Sivilotti, Lucia G ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; GLUTAMATE RECEPTOR; GLUTAMIC ACID DERIVATIVE; GLYCINE DERIVATIVE; NICOTINIC RECEPTOR; PROTEIN DERIVATIVE;

BINDING AFFINITY; BINDING SITE; CHANNEL GATING; CONFORMATIONAL TRANSITION; CORRELATION ANALYSIS; CRYSTAL STRUCTURE; EQUILIBRIUM CONSTANT; MEMBRANE PERMEABILITY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MECHANICS; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; TECHNIQUE;

ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HUMANS; ION CHANNEL GATING; ION CHANNELS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; PROTEIN CONFORMATION; RECEPTORS, GLUTAMATE; RECEPTORS, GLYCINE; RECEPTORS, NICOTINIC;

EID: 2542443504     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2004.04.010     Document Type: Review

References (70)

1. Fersht A.R. Characterizing transition states in protein folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 5:1995;79-84
2. Colquhoun D., et al. Nicotinic acetylcholine receptors. Abraham D. Burger's Medicinal Chemistry Drug Discovery and Drug Development. 6th edn:2003;357-405 John Wiley
3. Auerbach A. Life at the top: the transition state of AChR gating. Sci. STKE. 2003:2003;re11
4. Engel A.G., et al. Congenital myasthenic syndromes: progress over the past decade. Muscle Nerve. 27:2003;4-25
5. Unwin N. Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy. FEBS Lett. 555:2003;91-95
6. Miyazawa A., et al. Structure and gating mechanism of the acetylcholine receptor pore. Nature. 424:2003;949-955
7. Brejc K., et al. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature. 411:2001;269-276
8. Celie P.H., et al. Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron. 41:2004;907-914
9. Langosch D., et al. Conserved quaternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer. Proc. Natl. Acad. Sci. U. S. A. 85:1988;7394-7398
10. Kuhse J., et al. Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry. Neuron. 11:1993;1049-1056
11. Burzomato V., et al. Stoichiometry of recombinant heteromeric glycine receptors revealed by a pore-lining region point mutation. Receptors Channels. 9:2003;353-361
12. Laube B., et al. Molecular determinants of agonist discrimination by NMDA receptor subunits: Analysis of the glutamate binding site on the NR2B subunit. Neuron. 18:1997;493-503
13. Anson L.C., et al. Identification of amino acid residues of the NR2A subunit which control glutamate potency in recombinant NR1/NR2A NMDA receptors. J. Neurosci. 18:1998;581-589
14. Schorge S., Colquhoun D. Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits. J. Neurosci. 23:2003;1151-1158
15. Armstrong N., Gouaux E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron. 28:2000;165-181
16. Furukawa H., Gouaux E. Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22:2003;2873-2885
17. Grosman C., et al. Mapping the conformational wave of acetylcholine receptor channel gating. Nature. 403:2000;773-776
18. Cymes G.D., et al. Structure of the transition state of gating in the acetylcholine receptor channel pore: a φ-value analysis. Biochemistry. 41:2002;5548-5555
19. Chakrapani S., et al. The role of loop 5 in acetylcholine receptor channel gating. J. Gen. Physiol. 122:2003;521-539
20. Colquhoun D. Binding, gating, affinity and efficacy. The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br. J. Pharmacol. 125:1998;924-947
21. Colquhoun D., Sakmann B. Fluctuations in the microsecond time range of the current through single acetylcholine receptor ion channels. Nature. 294:1981;464-466
22. Colquhoun D., Sakmann B. Fast events in single-channel currents activated by acetylcholine and its analogues at the frog muscle end-plate. J. Physiol. 369:1985;501-557
23. Qin F., et al. Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events. Biophys. J. 70:1996;264-280
24. Colquhoun D., et al. Joint distributions of apparent open times and shut times of single ion channels and the maximum likelihood fitting of mechanisms. Philos. Trans. R. Soc. Lond. B Biol. Sci. 354:1996;2555-2590
25. Colquhoun D., et al. The quality of maximum likelihood estimates of ion channel rate constants. J. Physiol. 547:2003;699-728
26. Magleby K.L., Weiss D.S. Identifying kinetic gating mechanisms for ion channels by using two- dimensional distributions of simulated dwell times. Proc. R. Soc. Lond. B. Biol. Sci. 241:1990;220-228
27. Salamone F.N., et al. A re-examination of adult mouse nicotinic acetylcholine receptor channel activation kinetics. J. Physiol. 516:1999;315-330
28. Hatton C.J., et al. Properties of the human muscle nicotinic receptor, and of the slow-channel myasthenic syndrome mutant εL221F, inferred from maximum likelihood fits. J. Physiol. 547:2003;729-760
29. Beato M., et al. The activation mechanism of α1 homomeric glycine receptors. J. Neurosci. 24:2004;895-906
30. Beato M., et al. Openings of the rat recombinant α1 homomeric glycine receptor as a function of the number of agonist molecules bound. J. Gen. Physiol. 119:2002;443-466
31. Grosman C., Auerbach A. The dissociation of acetylcholine from open nicotinic receptor channels. Proc. Natl. Acad. Sci. U. S. A. 98:2001;14102-14107
32. Sine S.M., et al. Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts: single channel current kinetics reveal distinct agonist binding affinities. J. Gen. Physiol. 96:1990;395-437
33. Jackson M.B. Dependence of acetylcholine receptor channel kinetics on agonist concentration in cultured mouse muscle fibres. J. Physiol. 397:1988;555-583
34. Zhang Y., et al. Activation of recombinant mouse acetylcholine receptors by acetylcholine, carbamylcholine and tetramethylammonium. J. Physiol. 486:1995;189-206
35. Auerbach A., et al. Voltage dependence of mouse acetylcholine receptor gating: different charge movements in di-, mono- and unliganded receptors. J. Physiol. 494:1996;155-170
36. Wang H.L., et al. Mutation in the M1 domain of the acetylcholine receptor α subunit decreases the rate of agonist dissociation. J. Gen. Physiol. 109:1997;757-766
37. Milone M., et al. Slow-channel myasthenic syndrome caused by enhanced activation, desensitization, and agonist binding affinity attributable to mutation in the M2 domain of the acetylcholine receptor α subunit. J. Neurosci. 17:1997;5651-5665
38. Monod J., et al. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:1965;88-118
39. Burzomato, V., et al. (2004) Activation of heteromeric α1/β rat glycine receptors. Biophysical Society Abstracts 1497 (http://www. biophysics.org/abstracts/).
40. Jin R., et al. Structural basis for partial agonist action at ionotropic glutamate receptors. Nat. Neurosci. 6:2003;803-810
41. Popescu G., Auerbach A. Modal gating of NMDA receptors and the shape of their synaptic response. Nat. Neurosci. 6:2003;476-483
42. Banke T.G., Traynelis S.F. Activation of NR1/NR2B NMDA receptors. Nat. Neurosci. 6:2003;144-152
43. Gibb A.J., Colquhoun D. Glutamate activation of a single NMDA receptor-channel produces a cluster of channel openings. Proc. R. Soc. Lond. B. Biol. Sci. 243:1991;39-45
44. Wyllie D.J.A., et al. Single-channel activations and concentration jumps: comparison of recombinant NR1/NR2A and NR1/NR2D NMDA receptors. J. Physiol. 510:1998;1-18
45. del Castillo J., Katz B. Interaction at end-plate receptors between different choline derivatives. Proc. R. Soc. Lond. B. Biol. Sci. 146:1957;369-381
46. Colquhoun D., Ogden D.C. Activation of ion channels in the frog end-plate by high concentrations of acetylcholine. J. Physiol. 395:1988;131-159
47. Grosman C., Auerbach A. Asymmetric and independent contribution of the second transmembrane segment 12′ residues to diliganded gating of acetylcholine receptor channels. A single-channel study with choline as the agonist. J. Gen. Physiol. 115:2000;637-651
48. Gardner P., et al. Conductances of single ion channels opened by nicotinic agonists are indistinguishable. Nature. 309:1984;160-162
49. Lewis T.M., et al. Kinetic determinants of agonist action at the recombinant human glycine receptor. J. Physiol. 549:2003;361-374
50. Mortensen, M., et al. (2004) Activation of single heteromeric GABAA receptor ion channels by full and partial agonists. J.Physiol. [DOI: 10.1113/jphysiol.2003.054734].
51. Chen N., et al. Subtype-dependence of NMDA receptor channel open probability. J. Neurosci. 19:1999;6844-6854
52. Low C.M., et al. Molecular determinants of proton-sensitive N-methyl-D-aspartate receptor gating. Mol. Pharmacol. 63:2003;1212-1222
53. Traynelis S.F., Cull-Candy S.G. Proton inhibition of N-methyl-D-aspartate receptors in cerebellar neurons. Nature. 345:1990;347-350
54. Howe J.R., et al. Currents through single glutamate-receptor channels in outside-out patches from rat cerebellar granule cells. J. Physiol. 432:1991;143-202
55. McLarnon J.G., Sawyer D. Dependence of single channel properties of the N-methyl-D-aspartate ion channel on stereoisomer agonists. Exp. Brain Res. 95:1993;8-14
56. Rosenmund C., et al. The tetrameric structure of a glutamate receptor channel. Science. 280:1998;1596-1599
57. Smith T.C., Howe J.R. Concentration-dependent substate behavior of native AMPA receptors. Nat. Neurosci. 3:2000;992-997
58. Unwin N., et al. Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits. J. Mol. Biol. 319:2002;1165-1176
59. Gouaux E. Structure and function of AMPA receptors. J. Physiol. 554:2004;249-253
60. Shen X.M., et al. Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating. J. Clin. Invest. 111:2003;497-505
61. Grosman C., et al. The extracellular linker of muscle acetylcholine receptor channels is a gating control element. J. Gen. Physiol. 116:2000;327-339
62. Rajendra S., et al. Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists. Neuron. 14:1995;169-175
63. Lynch J.W., et al. Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel. EMBO J. 16:1997;110-120
64. Lewis T.M., et al. Properties of human glycine receptors containing the hyperekplexia mutation α1(K276E), expressed in Xenopus oocytes. J. Physiol. 507:1998;25-40
65. Shan Q., et al. Asymmetric contribution of α and β subunits to the activation of αβ heteromeric glycine receptors. J. Neurochem. 86:2003;498-507
66. Revah F., et al. Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor. Nature. 353:1991;846-849
67. Labarca C., et al. Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors. Nature. 376:1995;514-516
68. Chang Y., et al. Stoichiometry of a recombinant GABAA receptor. J. Neurosci. 16:1996;5415-5424
69. Boorman J.P., et al. Stoichiometry of human recombinant neuronal nicotinic receptors containing the β3 subunit expressed in Xenopus oocytes. J. Physiol. 529:2000;565-577
70. Wilson G.G., Karlin A. The location of the gate in the acetylcholine receptor channel. Neuron. 20:1998;1269-1281