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Pure β-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclase

Nature volume 306, pages 562–566 (1983)Cite this article

Abstract

The β-adrenergic receptor binding subunits from frog erythrocytes, hamster lung and guinea pig lung have been purified to apparent homogeneity and in all cases reside on a single polypeptide. Insertion of the pure receptors into phospholipid vesicles and subsequent fusion of these vesicles with a receptor-deficient cell conveys β-adrenergic responsiveness to the adenylate cyclase system of the acceptor cell. Such responsiveness is linearly dependent on the amount of receptor used in the fusion experiments and is independent of the receptor source. Moreover, this responsiveness displays appropriate β-adrenergic specificity. These results indicate that the β-adrenergic receptor polypeptide contains both the ligand binding site and the site responsible for mediating stimulation of adenylate cyclase activity, presumably via interaction with the guanine nucleotide regulatory protein.

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References

  1. Raftery, M. A., Vandlen, R. L., Reed, K. & Lee, T. Cold Spring Harb. Symp. quant. Biol. 40, 193–202 (1975).

    Article  Google Scholar 

  2. Jacobs, S., Schechter, Y., Bissel, K. & Cuatrecasas, P. Biochem. biophys. Res. Commun. 77, 981–988 (1977).

    Article  CAS  PubMed  Google Scholar 

  3. Kanellopoulos, J., Rossi, G. & Metzger, H. J. biol. Chem. 254, 7691–7697 (1979).

    CAS  PubMed  Google Scholar 

  4. Shorr, R. G. L. et al. Proc. natn. Acad. Sci. U.S.A. 79, 2778–2782 (1982).

    Article  ADS  CAS  Google Scholar 

  5. Shorr, R. G. L., Strohsacker, M. W., Lavin, T. N., Lefkowitz, R. J. & Caron, M. G. J. biol. Chem. 257, 12341–12350 (1982).

    CAS  PubMed  Google Scholar 

  6. Homcy, C. J., Rockson, S. G., Countaway, J. & Egan, D. A. Biochemistry 22, 660–668 (1983).

    Article  CAS  PubMed  Google Scholar 

  7. Sternweis, P. C., Northup, J. K., Smigel, M. D. & Gilman, A. J. biol. Chem. 256, 11517–11526 (1981).

    CAS  PubMed  Google Scholar 

  8. Hanski, E., Sternweis, P. C., Northup, J. K., Dromerick, A. W. & Gilman, A. G. J. biol. Chem. 256, 12911–12919 (1981).

    CAS  PubMed  Google Scholar 

  9. Caron, M. G. & Lefkowitz, R. J. J. biol. Chem. 256, 11944–11950 (1976).

    Google Scholar 

  10. Shorr, R. G. L., Lefkowitz, R. J. & Caron, M. G. J. biol. Chem. 256, 5820–5826 (1981).

    CAS  PubMed  Google Scholar 

  11. Caron, M. G., Srinivasan, Y., Pitha, J., Kociolek, K. & Lefkowitz, R. J. J. biol. Chem. 254, 2923–2927 (1979).

    CAS  PubMed  Google Scholar 

  12. Vauquelin, G., Geynet, P., Hanoune, J. & Strosberg, A. D. Proc. natn. Acad. Sci. U.S.A. 74, 3710–3714 (1977).

    Article  ADS  CAS  Google Scholar 

  13. Holloway, P. W. Analyt. Biochem. 53, 304–308 (1973).

    Article  CAS  PubMed  Google Scholar 

  14. Cerione, R. A. et al. Proc. natn. Acad. Sci. U.S.A. 80, 4899–4903 (1983)

    Article  ADS  CAS  Google Scholar 

  15. Eimerl, S., Neufield, G., Korner, M. & Schramm, M. Proc. natn. Acad. Sci. U.S.A. 77, 760–764 (1980).

    Article  ADS  CAS  Google Scholar 

  16. Strulovici, B., Stadel, J. M. & Lefkowitz, R. J. J. biol. Chem. 258, 6410–6414 (1983).

    CAS  PubMed  Google Scholar 

  17. Raftery, M. A., Hunkapiller, M. W., Strader, C. D. & Hood, L. E. Science 208, 1454–1457 (1980).

    Article  ADS  CAS  PubMed  Google Scholar 

  18. Conti-Tronconi, B. M. & Raftery, M. A. A. Rev. Biochem. 51, 491–530 (1982).

    Article  CAS  Google Scholar 

  19. Kasuga, M., Hedo, J. A., Yamada, K. M. & Kahn, C. R. J. biol. Chem. 257, 10392–10399 (1982).

    CAS  PubMed  Google Scholar 

  20. Obberghen, E. V., Rossi, B., Kowalski, A., Gazzano, H. & Ponzio, G. Proc. natn. Acad. Sci. U.S.A. 80, 945–949 (1983).

    Article  ADS  Google Scholar 

  21. Conrad, D. H. & Froese, A. J. Immun. 116, 319–326 (1976).

    CAS  PubMed  Google Scholar 

  22. Holowka, D., Gilter, C., Bercovici, T. & Metzger, H. Nature 289, 806–808 (1981).

    Article  ADS  CAS  PubMed  Google Scholar 

  23. Orly, J. & Schramm, M. Proc. natn. Acad. Sci. U.S.A. 73, 4410–4414 (1976).

    Article  ADS  CAS  Google Scholar 

  24. Pike, L. J. & Lefkowitz, R. J. Biochim. biophys. Acta 632, 354–365 (1980).

    Article  CAS  PubMed  Google Scholar 

  25. Pedersen, S. E. & Ross, E. M. Proc. natn. Acad. Sci. U.S.A. 79, 7228–7232 (1982).

    Article  ADS  CAS  Google Scholar 

  26. Stadel, J. M. et al. Proc. natn. Acad. Sci. U.S.A. 80, 3173–3177 (1983).

    Article  ADS  CAS  Google Scholar 

  27. Ames, N. B. & Dubin, D. T. J. biol. Chem. 235, 769–775 (1960).

    CAS  PubMed  Google Scholar 

  28. Schaffner, W. & Weissmann, C. Analyt. Biochem. 56, 502–514 (1973).

    Article  CAS  PubMed  Google Scholar 

  29. Schramm, M. Proc. natn. Acad. Sci. U.S.A. 76, 1174–1178 (1979).

    Article  ADS  CAS  Google Scholar 

  30. Korner, M., Gilon, C. & Schramm, M. J. biol. Chem. 257, 3389–3396 (1982).

    CAS  PubMed  Google Scholar 

  31. Lefkowitz, R. J. J. biol. Chem. 249, 6119–6124 (1974).

    CAS  PubMed  Google Scholar 

  32. Salomon, Y., Londos, C. & Rodbell, M. Analyt. Biochem. 58, 541–548 (1974).

    Article  CAS  PubMed  Google Scholar 

  33. Stadel, J. M. et al. J. biol. Chem. 258, 3032–3038 (1983).

    CAS  PubMed  Google Scholar 

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Authors and Affiliations

  1. Howard Hughes Medical Institute Research Laboratories, Departments of Medicine (Cardiology), Biochemistry and Physiology, Duke University Medical Center, Durham, North Carolina, 27710, USA

    Richard A. Cerione, Berta Strulovici, Jeffrey L. Benovic, Robert J. Lefkowitz & Marc G. Caron

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  1. Richard A. Cerione
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  2. Berta Strulovici
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  3. Jeffrey L. Benovic
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  4. Robert J. Lefkowitz
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  5. Marc G. Caron
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Cerione, R., Strulovici, B., Benovic, J. et al. Pure β-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclase. Nature 306, 562–566 (1983). https://doi.org/10.1038/306562a0

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