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Na+, K+-ATPase: relation of conformational transitions to function

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Summary

In its native environment, Na+, K+-ATPase of the plasma membrane is an oligomer consisting of two or more of each of two major subunits. Na+ and K+ move across the membrane through the channels that exist between the catalytic subunits of this oligomer. Two distinct ligand-induced conformational transitions (one due to the binding of K+ and ATP to the enzyme, and the other resulting from the phosphorylation of the enzyme in the presence of Na+ and ATP) cause changes in the geometries of the intersubunit channels, and provide the necessary energy-linked gating mechanisms for the transmembrane movements of ions against electrochemical gradients.

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References

  1. Glynn, I. M. & Karlish, S. J. D., 1975. Ann. Rev. Physiol. 37: 13–55.

    Google Scholar 

  2. Robinson, J. D. & Flashner, M. S., 1979. Biochim. Biophys. Acta 549: 145–176.

    Google Scholar 

  3. Schurmans, Stekhoven F. & Bonting, S. L., 1981. Physiol. Rev. 61: 1–76.

    Google Scholar 

  4. Schwartz, A., Lindenmayer, G. E. & Allen, J. C., 1975. Pharmacol. Rev. 27: 3–134.

    Google Scholar 

  5. Skou, J. C., 1957. Biochim. Biophys. Acta 23: 394–401.

    Article  CAS  PubMed  Google Scholar 

  6. Robinson, J. D., 1967. Biochemistry 6: 3250–3258.

    Google Scholar 

  7. Hart, W. M. & Titus, E. O., 1973. J. Biol. Chem. 248: 4674–4681.

    Google Scholar 

  8. Koepsell, H., 1979. J. Membrane Biol. 48: 69–94.

    Google Scholar 

  9. Glynn, I. M., Karlish, S. J. D. & Yates, D. W., 1979. In: Na, K-ATPase, Structure and Kinetics (Skou, J. C. & Norby, J. G., ed.) Academic Press, London, pp. 101–113.

  10. Jorgensen, P. L. & Petersen, J., 1979. In: Na, K-ATPase, Structure and Kinetics (Skou, J. C. & Norby, J. G., ed.) Academic Press, London, pp. 143–155.

  11. Jorgensen, P. L. & Karlish, J. D., 1980. Biochim. Biophys. Acta 597: 305–317.

    Google Scholar 

  12. Beauge, L. A. & Glynn, I. M., 1980. J. Physiol. 299: 367–383.

    Google Scholar 

  13. Karlish, S. J. D., 1979. In: Na, K-ATPase, Structure and Kinetics (Skou, J. D. & Norby, J. G., ed.) Academic Press, London, pp. 115–128.

  14. Karlish, S. J. D., 1980. J. Bioenerg. Biomembranes 12: 111–136.

    Google Scholar 

  15. Chetverin, A. B., Venyaminov, S. Y., Emelyanenko, V. I. & Burstein, E. A., 1980. Eur. J. Biochem. 188: 149–156.

    Google Scholar 

  16. Kuriki, Y., Halsey, J., Biltonen, R. & Racker, E., 1976. Biochemistry 15: 4965–4971.

    Google Scholar 

  17. Koepsell, H., 1979. J. Membrane Biol. 45: 1–20.

    Google Scholar 

  18. Huang, W. & Askari, A., 1979. FEBS Lett. 101: 67–70.

    Google Scholar 

  19. Askari, A., Huang, W. & Antieau, J. M., 1980. Biochemistry 19: 1132–1140.

    Google Scholar 

  20. Huang, W. & Askari, A., 1981. Biochim. Biophys. Acta, in press.

  21. Post, R. L., Sen, A. K. & Rosenthal, A. S., 1965. J. Biol. Chem. 240: 1437–1445.

    Google Scholar 

  22. Albers, R. W., Koval, G. J. & Seigel, G. L., 1968. Mol. Pharmacol. 4: 324–336.

    Google Scholar 

  23. Post, R. L., 1979. In: Cation Fluxes Across Biomembranes (Mukohata, Y. & Packer, L., ed.) Academic Press, New York, pp. 3–19.

  24. Stein, W. D. & Honig, B., 1977. Mol. Cell. Biochem. 15: 27–44.

    Google Scholar 

  25. Honig, B. & Stein, W. D., 1978. J. Theor. Biol. 75: 299–305.

    Google Scholar 

  26. Shamoo, A. E. & Ryan, T. E., 1975. Ann. N.Y. Acad. Sci. 264: 83–97.

    Google Scholar 

  27. Singer, S. J., 1974. Ann. Rev. Biochem. 43: 805–833.

    Google Scholar 

  28. Kyte, J., 1974. J. Biol. Chem. 249: 3652–3660.

    Google Scholar 

  29. Glynn, I. M., Karlish, S. J. D., Cavieres, J. D., Ellory, J. C., Lew, V. L. & Jorgensen, P. L., 1974. Ann. N.Y. Acad. Sci. 242: 357–371.

    Google Scholar 

  30. Askari, A., 1974. Ann. N.Y. Acad. Sci. 242: 372–388.

    Google Scholar 

  31. Yager, P., 1977. J. Theor. Biol. 66: 1–11.

    Google Scholar 

  32. Dunker, A. K. & Marvin, D. A., 1978. J. Theor. Biol. 72: 9–16.

    Google Scholar 

  33. Chandler, H. D., Woolf, C. J. & Hepburn, H. R., 1978. Biochem. J. 169: 559–565.

    Google Scholar 

  34. Reeves, A. S., Collins, J. H. & Schwartz, A., 1980. Biochem. Biophys. Res. Commun. 95: 1591–1598.

    Google Scholar 

  35. Spector, M., O'Neal, S. & Racker, E., 1980. J. Biol. Chem. 255: 8370–8373.

    Google Scholar 

  36. Rossi, B., Gache, C. & Lazdunski, M., 1978. Eur. J. Biochem. 85: 561–570.

    Google Scholar 

  37. Albers, R. W., Koval, G. J. & Swann, A. C., 1974. Ann. N.Y. Acad. Sci. 242: 268–279.

    Google Scholar 

  38. Askari, A., Huang, W. & Henderson, G. R., 1979. In: Na, K-ATPase, Structure and Kinetics (Skou, J. C. & Norby, J. G., ed.) Academic Press, London, pp. 205–215.

  39. Neet, K. E., 1980. Methods Enzymol. 64: 139–192.

    Google Scholar 

  40. Neet, K. E. & Ainsle, G. R., Jr., 1980. Methods Enzymol. 64: 192–226.

    Google Scholar 

  41. Levitzki, A. & Koshland, D. E., Jr., 1976. Curr. Top. Cell. Reg. 10: 1–40.

    Google Scholar 

  42. Yamaguchi, M. & Tonomura, Y., 1980. J. Biochem. 88: 1377–1385.

    Google Scholar 

  43. Matsui, H., Hayashi, Y., Homareda, H. & Kimimura, M., 1977. Biochem. Biophys. Res. Commun. 75: 373–380.

    Google Scholar 

  44. Yamaguchi, M. & Tonomura, Y., 1979. J. Biochem. 86: 509–523.

    Google Scholar 

  45. Yamaguchi, M. & Tonomura, Y., 1980. J. Biochem. 88: 1365–1375.

    Google Scholar 

  46. Hastings, D. & Skou, J. C., 1980. Biochim. Biophys. Acta 601: 380–385.

    Google Scholar 

  47. Craig, W. S. & Kyte, J., 1980. J. Biol. Chem. 255: 6262–6269.

    Google Scholar 

  48. Moczydlowski, E. G. & Fortes, P. A. G., 1981. J. Biol. Chem. 256: 2346–2356.

    Google Scholar 

  49. Moczydlowski, E. G. & Fortes, P. A. G., 1981. J. Biol. Chem. 256: 2357–2366.

    Google Scholar 

  50. Peters, W. H. M., Swarts, H. G. P., dePont, J. J. H. H. M., Schurmans, Stekhoven F. M. A. H. & Bonting, S. L., 1981. Nature 290: 338–339.

    Google Scholar 

  51. Skou, J. C. & Esmann, M., 1979. Biochim. Biophys. Acta 567: 436–444.

    Google Scholar 

  52. Askari, A. & Huang, W., 1981. FEBS Lett. 126: 215–218.

    Google Scholar 

  53. Patzelt-Wenczler, R. & Schoner, W., 1981. Eur. J. Biochem. 114: 79–87.

    Google Scholar 

  54. Hansen, O., Jensen, J., Norby, J. G. & Ottolenghi, P., 1979. Nature 280: 410–412.

    Google Scholar 

  55. Askari, A. & Huang, W., 1980. Biochem. Biophys. Res. Commun. 93: 448–453.

    Google Scholar 

  56. Deguchi, N., Jorgensen, P. L. & Maunsbach, A. B., 1977. J. Cell. Biol. 75: 619–634.

    Google Scholar 

  57. Maunsbach, A. B., Skriver, E. & Jorgensen, P. L., 1979. In: Na, K-ATPase, Structure and Kinetics (Skou, J. C. & Norby, J. G., ed.) Academic Press, London, pp. 3–13.

  58. Hasse, W. & Koepsell, H., 1979. Plugers Arch. 381: 127–135.

    Google Scholar 

  59. Peters, W. H. M., dePont, J. J. H. H. M., Koppers, A. & Bonting, S. L., 1981. Biochim. Biophys. Acta 641: 55–70.

    Google Scholar 

  60. Hastings, D. F. & Reynolds, J. A., 1979. Biochemistry 18: 817–821.

    Google Scholar 

  61. Esmann, M., Skou, J. C. & Christiansen, C., 1979. Biochim. Biophys. Acta 567: 410–420.

    Google Scholar 

  62. Esman, M., Christiansen, C., Karlsson, K., Hnsson, G. C. & Skou, J. C., 1980. Biochim. Biophys. Acta 603: 1–12.

    Google Scholar 

  63. Neufeld, A. H. & Levy, H. M., 1969. J. Biol. Chem. 244: 6493–6497.

    Google Scholar 

  64. Post, R. L., Hegyvary, C. & Kume, S., 1972. J. Biol. Chem. 247: 6530–6540.

    Google Scholar 

  65. Stein, W. D., Lieb, W. R., Karlish, S. J. D. & Eilam, Y., 1973. Proc. Nat. Acad. Sci., U.S.A. 70: 275–278.

    Google Scholar 

  66. Repke, K. R. H. & Schon, R., 1973. Acta Biol. Med. Germ. 31: K19-K30.

    Google Scholar 

  67. Harada, K. & Wolfe, R. G., 1968. J. Biol. Chem. 4123.

  68. Lazdunski, M., 1970. Curr. Top. Cell. Regul. 6: 267–310.

    Google Scholar 

  69. Smith, R. L., Zinn, K. & Cantley, L. C., 1980. J. Biol. Chem. 255: 9852–9859.

    Google Scholar 

  70. Stein, W. D., 1979. In: Na, K-ATPase, Structure and Kinetics (Skou, J. C. & Norby, J. G., ed.) Academic press, London, pp. 475–486.

  71. Repke, K. R. H. & Dittrich, F., 1979. In: Na, K-ATPase, Structure & Kinetics (Skou, J. C. & Norby, J. G., ed.) Academic Press, London, pp. 487–500.

  72. Boyer, P. D., 1974. In: Dynamics of Energy Transducing Membrane (Ernster, L. & Estabrook, R. W. & Slater, E. C., ed.) BBA Libr. Vol. 13, pp. 289–301.

  73. Boyer, P. D., 1975. FEBS Lett. 50: 91–94.

    Google Scholar 

  74. Boyer, P. D., 1977. Ann. Rev. Biochem. 46: 957–966.

    Google Scholar 

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Askari, A. Na+, K+-ATPase: relation of conformational transitions to function. Mol Cell Biochem 43, 129–143 (1982). https://doi.org/10.1007/BF00223005

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