Skip to main content
Log in

The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors

  • Article
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

We have cloned and sequenced cDNAs of the strychnine-binding subunit of the rat glycine receptor, a neurotransmitter-gated chloride channel protein of the CNS. The deduced polypeptide shows significant structural and amino-acid sequence homology with nicotinic acetylcholine receptor proteins, indicating that there is a family of genes encoding neurotransmitter-gated ion channels.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. 1. Popot, J. L. & Changeux, J. P. Physiol. Rev. 64, 1162–1239 (1984). 2. Stroud, R. M. & Finer–Moore J. A. Rev. Cell Biol. 1, 317–351 (1985). 3. Noda, M. el al Nature 305, 818–823 (1983). 4. Boulter, J. et al. Nature 319, 368–374 (1986). 5. Krnjevic, K. Physiol Rev. 54, 418–540 (1974). 6. Coombs, J. S., Eccles, J. C. & Fatt, P. J. Physiol, Lond. 130, 326–373 (1955). 7. Aprison, M. H. & Werman, R. Life Sci. 4, 2075–2083 (1965). 8. Young, A. B. & Snyder, S. H. Proc. natn. Acad. Sci. U.S.A. 70, 2832–2836 (1973). 9. Zarbin, M. A., Wamsley, J. K. & Kuhar, M. J. / Neurosci. 1, 532–547 (1981). 10. Probst, A., Cortes, R. & Palacios, J. M. Neuroscience 17, 11–35 (1986). 11. Hall, P. V., Smith, J. E., Lane, J., Mote, J. & Campbell, R. Neurology 29, 262–267 (1979). 12. White, W. F. & Heller, A. H. Nature 298, 655–657 (1982). 13. Hayashi, H., Suga, M., Satake, M. & Tsubaki, T. Ann. Neurol. 9, 292–294 (1981). 14. Lloyd, K. G., De Mentis, G., Broekkamp, C. L., Thuret, F. & Worms, P. Adv. biochem. 49. Psychopharmac. 37, 137–148 (1983). 15. Pfeiffer, F., Graham, D. & Betz, H. J. biol Chem. 257, 9389–9393 (1982). 16. Graham, D., Pfeiffer, F. & Betz, H. Biochemistry 24, 990–994 (1985). 17. Becker, C.–M., Hermans–Borgmeyer, I., Schmitt, B. & Betz, H. /. Neurosci. 6, 1358–1364 53. (1986). 18. Graham, D., Pfeiffer, F. & Betz, H. Biochem. biophys. Res. Commun. 102,1330–1335 (1981). 19. Graham, D., Pfeiffer, F. & Betz, H. Eur. J. Biochem. 131, 519–525 (1983). 20. Schmitt, B., Knaus, P., Becker, C.–M. & Betz, H. Biochemistry 26, 805–811 (1987). 21. Pfeiffer, F., Simler, R., Grenningloh, G. & Betz, H. Proc. natn. Acad. Sci. U.S.A. 81,7224–7227 (1984). 22. Betz, H. Naturwissenschaften 71, 363–368 (1984). 23. Betz, H. Trends Neurosci. 10, 113–117 (1987). 24. Triller, A., Cluzeaud, F., Pfeiffer, F., Betz, H. & Korn, H. J. Cell Biol. 101, 683–688 (1985). 25. Altschuler, R. A., Betz, H., Parakkal, M. H., Reeks, K. A. & Wenthold, R. J. Brain Res. 60. 369, 316–320 (1986). 26. Simikawa, K., Parker, I. & Miledi, R. Proc. natn. Acad. Sci. U.S.A. 81, 7994–7998 (1984). 27. Kawasaki, E. S. Nucleic Acids Res. 13, 4991–5004 (1985). 28. Lathe, R. /. molec. Biol. 183, 1–12 (1985). 29. Benavides, J., Lopez–Lahoya, J., Valdivieso, F. & Ugarte M. /. Neurochem. 37, 315–320 63. (1981). 30. Hortsch, M. & Meyer, D. I. Int. Rev. Cytol. 102, 215–245 (1986). 31. Hopp, T. P. & Woods, K. R. Proc. natn. Acad. Sci. U.S.A. 78, 3824–3828 (1981). 32. La Polla, R. J., Mixter–Mayne, K. N. & Davidson, N. Proc. natn. Acad. Sci. U.S.A. 81, 66. 7970–7974 (1984). 33. Kubo, T. et al. Eur. J. Biochem. 149, 5–13 (1985). 34. Nef, P., Mauron, A., Stadler, R., Alliod, C. & Ballivet, M. Proc. natn. Acad. Sci. U.S.A. 81, 7975–7979 (1984). 35. Boulter, J. et al. J. Neurosci. 5, 2545–2552 (1985). 36. Hermans–Borgmeyer, I. et al. EMBO J. 5, 1503–1508 (1986). 37. Numa, S. Biochem. Soc. Symp. 52, 119–143 (1986). 38. Goldman, D. et al Cell 48, 965–973 (1987). 39. Mishina, M. et al Nature 313, 364–369 (1985). 40. Imoto, K. et al. Nature 324, 670–674 (1986). 41. Giraudat, J., Dennis, M., Heidmann, T., Chang, J.–Y. & Changeux, J.–P. Proc. natn. Acad. Sci. U.S.A. 83, 2719–2723 (1986). 42. Oberthur, W. et al. EMBO J. 5, 1815–1819 (1986). 43. Brandl, C. J. & Deber, C. M. Proc. natn. Acad. Sci. U.S.A. 83, 917–921 (1986). 44. Bormann, J., Hamill, O. P. & Sakmann, B. /. Physiol., Lond. 385, 243–286 (1987). 45. Faber, D. S. & Korn, H. J. Neurosci. 7, 807–811 (1987). 46. Gold, M. R. & Martin, A. R. Nature 299, 828–830 (1982). 47. Pfeiffer, F. & Betz, H. Brain Res. 226, 273–279 (1981). 48. Young, A. B. & Snyder, S. H. Molec. Pharmac. 10, 790–809 (1974). 49. Kao, P. N. et al. J. biol Chem. 259, 11662–11665 (1984). 50. Noda, M. et al Nature 299, 793–797 (1982). 51. Dixon, R. A. F. et al. Nature 321, 75–79 (1986). 52. Kubo, T. et al Nature 323, 411–416 (1986). 53. Methfessel, C. et al Pflugers Arch. ges. Physiol. (in the press). 54. Sinha, N. D., Biernat, J., McManns, J. & Kosters, H. Nucleic Acids Res. 12, 4539–4557 (1984). 55. Laemmli, U.K. Nature 227, 680–685 (1970). 56. Cleveland, D. W., Fischer, S. G., Kirschner, M. W. & Laemmli, U.K. J. biol. Chem. 252, 1102–1106 (1977). 57. Hewick, R. M., Hunkapiller, M. W., Hood, L. E. & Dreyer, W. J. J. biol. Chem. 256, 7990–7997 (1981). 58. Bassiri, R. M. & Utiger, R. D. Endocrinology 90, 722–727 (1971). 59. Kaplan, B. B., Bernstein, S. L. & Gioio, A. Biochem. J. 183, 181–184 (1979). 60. Aviv, H. & Leder, P. Proc. natn. Acad. Sci. U.S.A. 69, 1408–1412 (1972). 61. Maniatis, T., Fritsch, E. F. & Sambrook, J. Molecular Cloning, A Laboratory Manual (Cold Spring Harbour Laboratory, New York, 1982). 62. Huynh, T. V., Young, R. A. & Davis, R. W. in DNA Cloning, a Practical Approach Vol. 1 (ed. Glover, D. M.) 49–78 (IRL, Oxford, 1984). 63. Mason, P. J. & Williams, J. G. Nucleic Acid Hybridization, a Practical Approach (eds Hames, D. & Higgins, J.) 113–137 (IRL, Oxford, 1985). 64. Norrander, J., Kempe, T. & Messing, J. Gene 26, 101–106 (1983). 65. Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977). 66.Thomas, P. S. Proc. natn. Acad. Sci. U.S.A. 77, 5201–5205 (1980). 67. Dayhoff, M. O., Schwartz, R. M. & Orcutt, B. C. in Atlas of Protein Sequence and Structure Vol. 5, suppl. 3 (ed. Dayhoff, M. O.) 345–352 (National Biomedical Research Foundation, Silver Spring, Maryland, 1978). 68. Hubbard, S. C. & Ivatt, R. J. A. Rev. Biochem. 50, 555–583 (1981).

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Grenningloh, G., Rienitz, A., Schmitt, B. et al. The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors. Nature 328, 215–220 (1987). https://doi.org/10.1038/328215a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/328215a0

  • Springer Nature Limited

This article is cited by

Navigation