Acetylcholine receptor M3 domain: Stereochemical and volume contributions to channel gating

Nature Neuroscience

Volumn 2, Issue 3, 1999, Pages 226-233

  Wang, Hai Long ^a   Milone, Margherita ^b   Ohno, Kinji ^a   Shen, Xing Ming ^a   Tsujino, Akira ^a   Batocchi, Anna Paola ^b   Tonali, Pietro ^b   Brengman, Joan ^a   Engel, Andrew G ^a   Sine, Steven M ^a  

^a MAYO CLINIC   (United States)

^b CATHOLIC UNIVERSITY   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

MUSCARINIC M3 RECEPTOR;

ARTICLE; CASE REPORT; CHANNEL GATING; ENDPLATE POTENTIAL; GENE FUNCTION; GENE MUTATION; HUMAN; MALE; MYASTHENIA GRAVIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DOMAIN; REGULATORY MECHANISM; SCHOOL CHILD; STEREOCHEMISTRY;

AMINO ACID SEQUENCE; CHILD; DNA MUTATIONAL ANALYSIS; HUMANS; ION CHANNEL GATING; ION CHANNELS; KINETICS; MALE; MOLECULAR SEQUENCE DATA; NEUROMUSCULAR DISEASES; RECEPTORS, CHOLINERGIC; STEREOISOMERISM; SYNDROME;

EID: 0033363317     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/6326     Document Type: Article

References (33)

1. Changeux, J. P. Functional architecture and dynamics of the nicotinic acetylcholine receptor, an allosteric ligand-gated ion channel. Fida Res. Found. Neurosci. Award Lect. 4, 21-168 (1990).
2. Engel, A. G., Ohno, K., Wang, H.-L., Milone, M. & Sine, S. M. Molecular basis of congenital myasthenic syndromes: Mutations in the acetylcholine receptor. Neuroscientist 4, 185-194 (1998).
3. Plomp, J. J., van Kempen, G. T. H. & Molenaar, P. C. Adaptation of quantal content to decreased postsynaptic sensitivity at single endplates in α-bungarotoxin treated rats. J. Physiol. (Lond.) 458, 487-499 (1992).
4. Plomp, J. J. et al. Acetylcholine release in myasthenia gravis: Regulation at single end-plate level. Ann. Neurol. 37, 627-636 (1995).
5. Ohno, K. et al. Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor ε subunit. Neuron 17, 157-170 (1996).
6. Sakmann, B., Patlak, J. & Neher, E. Single acetylcholine-activated channels show burst-kinetics in the presence of desensitising concentrations of agonist. Nature 286, 71-73 (1980).
7. Sine, S., Claudio, T. & Sigworth, F. Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts: single channel current kinetics reveal distinct agonist binding affinities. J. Gen. Physiol. 96, 395-437 (1990).
8. Milone, M. et al. Mode switching kinetics produced by a naturally occurring mutation in the cytoplasmic loop of the human acetylcholine receptor ε subunit. Neuron 20, 575-588 (1998).
9. Horn, R. & Lange, K. Estimating kinetic constants from single channel data. Biophys. J. 43, 207-223 (1983).
10. Qin, F., Auerbach, A. & Sachs, F. Estimating single-channel kinetic parameters from idealized patch clamp data containing missed events. Biophys. J. 70, 264-280 (1996).
11. Magleby, K. L. in Myology 2nd edn (eds. Engel, A. G. & Franzini-Armstrong, C.) 442-463 (McGraw-Hill, New York, 1994).
12. Unwin, N. Nicotinic acetylcholine receptor at 9Å resolution. J. Mol. Biol. 229, 1101-1124 (1993).
13. Charnet, P. et al. An open channel blocker interacts with adjacent turns of α-helices in the nicotinic acetylcholine receptor. Neuron 2, 87-95 (1990).
14. Akabas, M., Kaufmann, C., Archdeacon, P. & Karlin, A. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit. Neuron 13, 919-927 (1994).
15. Blanton, M. & Cohen, J. Identifying the lipid-protein interface of the Torpedo nicotinic acetylcholine receptor: secondary structure implications. Biochemistry 33, 2859-2872 (1994).
16. Gorne-Tschelnoko, U., Strecker, A., Kaduk, C., Naumann, D. & Hucho, F. The transmembrane domains of the nicotinic acetylcholine receptor contain alpha helical and beta structures. EMBO J. 13, 338-341 (1994).
17. Ortells, M. & Lunt, G. A mixed helix-beta-sheet model of the transmembrane region of the nicotinic acetylcholine receptor. Protein Eng. 9, 51-59 (1996).
18. Fambrough, D. M., Engel, A. G. & Rosenberry, T. L. Acetylcholinesterase of human erythrocytes and neuromuscular junctions: Homologies revealed by monoclonal antibodies. Proc. Natl. Acad. Sci. USA 79, 1078-1082 (1982).
19. Engel, A. G. in Myology: Basic and Clinical 2 edn (eds. Engel, A. G. & Franzini-Armstrong, C.) 822-831 (McGraw-Hill, New York, 1994).
20. Engel, A. G., Lindstrom, J. M., Lambert, E. H. & Lennon, V. A. Ultrastructural localization of the acetylcholine receptor in myasthenia gravis and in its experimental autoimmune model. Neurology 27, 307-315 (1977).
21. Engel, A. G., Nagel, A., Walls, T. J., Harper, C. M. & Waisburg, H. A. Congenital myasthenic syndromes. I. Deficiency and short open-time of the acetylcholine receptor. Muscle Nerve 16, 1284-1292 (1993).
22. Uchitel, O. et al. Congenital myasthenic syndromes. II. A syndrome attributed to abnormal interaction of acetylcholine with its receptor. Muscle Nerve 16, 1293-1301 (1993).
23. Milone, M., Hutchinson, D. O. & Engel, A. G. Patch-clamp analysis of the properties of acetylcholine receptor channels at the normal human endplate. Muscle Nerve 17, 1364-1369 (1994).
24. Colquhoun, D. & Sakmann, B. Fast events in single channel currents activated by acetylcholine and its analogues at the frog muscle end-plate. J. Physiol. (Lond.) 369, 501-557 (1985).
25. Sigworth, F. J. & Sine, S. M. Data transformation for improved display and fitting of single-channel dwell time histograms. Biophys. J. 52, 1047-1054 (1987).
26. Sambrook, J., Fritsch, E. F. & Maniatis, T. Molecular Cloning: A Laboratory Manual, 2 edn (Cold Spring Harbor Lab. Press, Plainview, New York, 1989).
27. Ohno, K. et al. Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the ε subunit. Proc. Natl. Acad. Sci. USA 92, 758-762 (1995).
28. Luther, M. A. et al. A muscle acetylcholine receptor is expressed in the human cerebellar medulloblastoma cell line TE671. J. Neurosci. 9, 1082-1096 (1989).
29. Schoepfer, R., Luther, M. & Lindstrom, J. The human medulloblastoma cell line TE671 expresses a muscle-like acetylcholine receptor. Cloning of the alpha-subunit cDNA. FEBS Lett. 226, 235-240 (1988).
30. Lee, B. S., Gunn, R. B. & Kopito, R. R. Functional differences among nonerythroid anion exchangers expressed in a transfected human cell line. J. Biol. Chem. 266, 11448-11454 (1991).
31. Ohno, K. et al. Congenital myasthenic syndromes due to heteroallelic nonsense/missense mutations in the acetylcholine receptor ε subunit gene: identification and functional characterization of six new mutations. Hum. Mol. Genet. 6, 753-766 (1997).
32. Bouzat, C., Bren, N. & Sine, S. M. Structural basis of different gating kinetics of fetal and adult acetylcholine receptors. Neuron 13, 1395-1402 (1994).
33. 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, 757-766 (1997).