Abstract
The complete amino-acid sequence of the receptor for dihydropyridine calcium channel blockers from rabbit skeletal muscle is predicted by cloning and sequence analysis of DNA complementary to its messenger RNA. Structural and sequence similarities to the voltage-dependent sodium channel suggest that in the transverse tubule membrane of skeletal muscle the dihydropyridine receptor may act both as voltage sensor in excitation-contraction coupling and as a calcium channel
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
1. Reuter, H. Nature 316, 391 (1985). 2. Reuter, H., Porzig, H., Kokubun, S. & Prod'hom, B. Trends Neurosci. 8, 396–400 (1985). 3. Curtis, B. M. & Catterall, W. A. Biochemistry 23, 2113–2118 (1984). 4. Borsotto, M., Barhanin, J., Norman, R. I. & Lazdunski, M. Biochem. biophys. Res. Commun. 122, 1357–1366 (1984). 5. Flockerzi, V., Oeken, H.–J. & Hofmann, F. Eur. J. Biochem. 161, 217–224 (1986). 6. Vandaele, S., Fosset, M., Galizzi, J.–P. & Lazdunski, M. Biochemistry 26, 5–9 (1987). 7. Noda, M. et al Nature 312, 121–127 (1984). 8. Noda, M. et al. Nature 320, 188–192 (1986). 9. Curtis, B. M. & Catterall, W. A. Proc. natn. Acad. Sci. U.S.A. 82, 2528–2532 (1985). 10. Hosey, M. M., Borsotto, M. & Lazdunski, M. Proc. natn. Acad. Sci. U.S.A. 83, 3733–3737 (1986). 11. Galizzi, J.–P., Borsotto, M., Barhanin, J., Fosset, M. & Lazdunski, M. J. biol Chem. 261, 1393–1397 (1986). 12. Kozak, M. Nucleic Acids Res. 12, 857–872 (1984). 13. Grefrath, S. P. & Reynolds, J. A. Proc. natn. Acad. Sci. U.S.A. 71, 3913–3916 (1974). 14. Toh, H., Hayashida, H. & Miyata, T. Nature 305, 827–829 (1983). 15. Hubbard, S. C. & Ivatt, R. J. A Rev. Biochem. 50, 555–583 (1981). 16. Krebs, E. G. & Beavo, J. A. A Rev. Biochem. 48, 923–959 (1979). 17. Noda, M. et al. Nature 322, 826–828 (1986). 18. Stiihmer, W., Methfessel, C., Sakmann, B., Noda, M. & Numa, S. Eur. Biophys. J. 14, 131–138 (1987). 19. Flockerzi, V. et al. Nature 323, 66–68 (1986). 20. Curtis, B. M. & Catterall, W. A. Biochemistry 25, 3077–3083 (1986). 21. McCleskey, E. W. & Aimers, W. Proc. natn. Acad. Sci. U.S.A. 82, 7149–7153 (1985). 22. Hess, P. & Tsien, R. W. Nature 309, 453–456 (1984). 23. Aimers, W. & McCleskey, E. W. /. PhysioL, Lond. 353, 585–608 (1984). 24. Kretsinger, R. H. A. Rev. Biochem. 45, 239–266 (1976). 25. Stuart, D. I. et al. Nature 324, 84–87 (1986). 26. Geisow, M. J., Fritsche, U., Hexham, J. M., Dash, B. & Johnson, T. Nature 320, 636–638 (1986). 27. Miller, R. J. & Freedman, S. B. Life Sci. 34, 1205–1221 (1984). 28. Schwartz, L. M., McCleskey, E. W. & Aimers, W. Nature 314, 747–751 (1985). 29. Rios, E. & Brum, G. Nature 325, 717–720 (1987). 30. Melzer, W., Schneider, M. F., Simon, B. J. & Szucs, G. / PhysioL, Lond. 373,481–511 (1986). 31. Pincon–Raymond, M., Rieger, F., Fossett, M. & Lazdunski, M. Devl Biol 112, 458–466 (1985). 32. Beam, K. G., Knudson, C. M. & Powell, J. A. Nature 320, 168–170 (1986). 33. Powell, J. A. & Fambrough, D. M. /. cell. Physiol. 82, 21–38 (1973). 34. Laemmli, U. K. Nature 227, 680–685 (1970). 35. Ferry, D. R., Rombusch, M., Goll, A. & Glossmann, H. FEBS Lett. 169, 112–118 (1984). 36. Kawakami, K. et al. Nature 316, 733–736 (1985). 37. Okayama, H. & Berg, P. Molec. cell. Biol. 2, 161–170 (1982). 38. Berk, A. J. & Sharp, P. A. Cell 12, 721–732 (1977). 39. Kadonaga, J. T., Jones, K. A. & Tjian, R. Trends biochem. Sci. 11, 20–23 (1986). 40. Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980). 41. Kyte, J. & Doolittle, R. F. J. molec. Biol 157, 105–132 (1982). 42. Chou, P. Y. & Fasman, G. D. A. Rev. Biochem. 47, 251–276 (1978).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Tanabe, T., Takeshima, H., Mikami, A. et al. Primary structure of the receptor for calcium channel blockers from skeletal muscle. Nature 328, 313–318 (1987). https://doi.org/10.1038/328313a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/328313a0
This article is cited by
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
