Skip to main content
SpringerLink
Log in

Interaction of Na,K-ATPase Catalytic Subunit with Cellular Proteins and Other Endogenous Regulators

  • Published:
Biochemistry (Moscow) Aims and scope Submit manuscript

Abstract

Some mechanisms of regulation of Na,K-ATPase activity in various tissues including the phosphorylation of the catalytic subunit of the enzyme by different protein kinases (PKA, PKC, and tyrosine kinase) and the interaction of the α-subunit with different proteins (Na,K-ATPase β- and γ-subunits, ankyrin, phosphoinositide-3 kinase, and AP-2 protein) and endogenous digitalis-like factors are considered. Special attention is given to the search for possible protein-partners including melittin-like protein and to the mechanism of enzyme regulation connected with the change of Na,K-ATPase quaternary structure. A recently discovered role of Na,K-ATPase as a receptor providing signal transduction inside the cell not only by changing the concentration of biologically significant cations but also using direct interaction of the enzyme with the protein-partners is discussed.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

REFERENCES

  1. Moller, J., Juul, D., and le Maire, M. (1996) Biochim. Biophys. Acta, 1286, 1–51.

    Google Scholar 

  2. Fambrough, D., Lemas, V., Takeyasu, K., Renaud, K. J., and Inman, E. M. (1994) Current Topics in Membranes, 41, 45–69.

    Google Scholar 

  3. Lopina, O. D (1999) Biol. Membr. (Moscow), 16, 584–603.

    Google Scholar 

  4. Therein, A., and Blostein, R. (2000) Am. J. Physiol., 279, C541-C566.

    Google Scholar 

  5. Sarvazyan, N. A., Modynov, N. N., and Askari, A. (1995) J. Biol. Chem., 95, 270, 26528–26532.

    Google Scholar 

  6. Luzhkov, V. B., and Surkov, N. F. (1998) J. Mol. Model., 4, 61–72.

    Google Scholar 

  7. Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature, 405, 647–655.

    Google Scholar 

  8. Kirley, T. (1989) J. Biol. Chem., 264, 7185–7192.

    Google Scholar 

  9. Schalzing, G., and Gloor, S. (1994) Cell Physiol. Biochem., 4, 96–114.

    Google Scholar 

  10. Beggah, A. T., Beguin, P., Jaunin, P., Peitsch, M. C., and Horisberger, J. D. (1993) Biochemistry, 32, 14117–14124.

    Google Scholar 

  11. Askari, A. (2000) in Na,K-ATPase and Related ATPases ( Taniguch, K., and Kaya, S., eds.) Elsevier Science, Amsterdam, pp. 17–26.

    Google Scholar 

  12. Askari, A. (1987) J. Bioenerg. Biomembr., 19, 359–374.

    Google Scholar 

  13. Periyasama, S. M., Huang, W.-Y., and Askari, A. (1983) J. Biol. Chem., 258, 9878–9885.

    Google Scholar 

  14. Koster, J. C., Blanko, G., and Mercer, R. W. (1995) J. Biol. Chem., 270, 14332–14339.

    Google Scholar 

  15. Hayashi, Y., Mimura, K., Matsui, H., and Takagi, T. (1989) Biochim. Biophys. Acta, 983, 217–229.

    Google Scholar 

  16. Mimura, K., Matsui, H., Takagi, T., and Hayashi, Y. (1993) Biochim. Biophys. Acta, 1145, 63–74.

    Google Scholar 

  17. Hayashi, Y., Kameyama, K., Kobayashi, T., Hagiwara, E., Shinji, N., and Takagi, T. (1997) Ann. N. Y. Acad. Sci., 834, 19–29.

    Google Scholar 

  18. Erdmann, E., and Hasse, W. (1975) J. Physiol. (London), 251, 671–682.

    Google Scholar 

  19. Jorgensen, P. L. (1982) Biochim. Biophys. Acta, 694, 27–68.

    Google Scholar 

  20. Kabakov, A. Yu. (1994) J. Theor. Biol., 169, 51–64.

    Google Scholar 

  21. Akera, T., and Ng, Y. C. (1991) Life. Sci., 18, 135–142.

    Google Scholar 

  22. Moore, E. D., Etter, E. F., Philipson, K. D., Carrington, W. A., Fogarty, K. E., Lifshitz, L. M., and Fay, F. S. (1993) Nature, 365, 657–660.

    Google Scholar 

  23. Avkiran, M., and Snabaitis, A. K. (1999) J. Thromb. Thrombolysis, 8, 25–32.

    Google Scholar 

  24. Greger, R. (2000) Am. J. Med. Sci., 319, 51–62.

    Google Scholar 

  25. Nelson, W. J., and Veshnock, P. (1987) Nature, 328, 533–537.

    Google Scholar 

  26. Shank, B. B., and Smith, N. E. (1976) J. Cell. Physiol., 87, 377–387.

    Google Scholar 

  27. Schneider, J. W., Mercer, R. W., Caplan, M., Emanuel, J. R., Sweadner, K. J., Benz, E. J., Jr., and Levenson, R. (1985) Proc. Natl. Acad. Sci. USA, 82, 6357–6361.

    Google Scholar 

  28. Shull, G. E., Greeb, J., and Lingrel (1986) Biochemistry, 25, 8125–8132.

    Google Scholar 

  29. Sverdlov, E. D., Monastyrskaya, G. S., Broude, N. E., Ushkaryov, Yu. A., Allikmets, R. L., Melkov, A. M., Smirnov, Yu. V., Malyshev, I. V., Dulobova, I. E., and Petrukhin, K. E. (1987) FEBS Lett., 217, 275–278.

    Google Scholar 

  30. Shamraj, O. I., and Lingrel, J. B. (1994) Proc. Natl. Acad. Sci. USA, 91, 12952–12956.

    Google Scholar 

  31. Blanko, G., Melton, R., Sanchez, G., and Mercer, R. W. (1999) Biochemistry, 38, 13661–13669.

    Google Scholar 

  32. Martin-Vasallo, P., Dackowski, W., Emanuel, J. R., and Levenson, R. (1989) J. Biol. Chem., 264, 4613–4618.

    Google Scholar 

  33. Gloor, S., Antonicek, Sweadner, K. J., Pagliusi, S., Frank, R., Moos, M., and Schachner, M. (1990) J. Cell. Biol., 110, 165–174.

    Google Scholar 

  34. Malik, N., Canfield, V. A., Backers, M. C., Gros, P., and Levenson, R. (1996) J. Biol. Chem., 271, 22754–22758.

    Google Scholar 

  35. Besirli, C. G., Gong, T. W., and Lomax, M. I. (1997) Biochim. Biophys. Acta, 1350, 21–26.

    Google Scholar 

  36. Blanko, G., Koster, J. C., Sanchez, G., and Mercer, R. W. (1995) Biochemistry, 34, 319–325.

    Google Scholar 

  37. Mobasheri, A., Avila, J., Cozar-Castellano, I., Brownleder, M. D., Trevan, M., Francis, M. J., Lamb, J. F., and Martin-Vasallo, P. (2000) Biosci. Rep., 20, 51–91.

    Google Scholar 

  38. Sweadner, K. J. (1989) Biochim. Biophys. Acta, 988, 185–220.

    Google Scholar 

  39. Barlet-Bas, C., Arystarkhova, E., Cheval, Marsy, S., Sweadner, K. J., Modyanov, N., and Doucet, A. (1993) J. Biol. Chem., 268, 11512–11515.

    Google Scholar 

  40. Bertorello, A. M., Aperia, A., Walaas, S. I., Nairn, A. C., and Greengard, P. (1991) Proc. Natl. Acad. Sci. USA, 88, 11359–11362.

    Google Scholar 

  41. Chibalin, A. V., Vasilets, L. A., Hennekes, H., Pralong, D., and Geering, K. (1992) J. Biol. Chem., 267, 22378–22384.

    Google Scholar 

  42. Chibalin, A. V., Lopina, O. D., Petukhov, S. P., and Vasilets, L. A. (1993) J. Bioenerg. Biomembr., 25, 61–66.

    Google Scholar 

  43. Feschenko, M. S., and Sweadner, K. J. (1994) J. Biol. Chem., 269, 30436–30444.

    Google Scholar 

  44. Fisone, G., Cheng, S., Nairn, A. C., Czernik, A. J., Hemmings, H. C., Hoog, J.-O., Bertorello, A. M., Kaizer, R., Bergman, T., Jornvall, H., Aperia, A., and Greengard, P. (1994) J. Biol. Chem., 269, 9368–9373.

    Google Scholar 

  45. Beguin, P., Beggah, A. T., Chibalin, A. V., Burgener-Kairuz, P., Jasser, F., Mathews, P. M., Rossier, B. C., Cottecchia, S., and Geering, K. (1994) J. Biol. Chem., 269, 24437–24445.

    Google Scholar 

  46. Cornelius, F., and Logvinenko, N. (1996) FEBS Lett., 380, 277–280.

    Google Scholar 

  47. Murtazina, D. A., Petukhov, S. P., Rubtsov, A. M., Storey, K. B., and Lopina, O. D. (2001) Biochemistry (Moscow), 66, 865–874.

    Google Scholar 

  48. Kurihara, K., Nakanishi, N., and Ueha, T. (2000) Am. J. Physiol., 279, C1516-C1527.

    Google Scholar 

  49. Fotis, H., Tatjanenko, L. V., and Vasilets, L. A. (1999) Eur. J. Biochem., 260, 904–910.

    Google Scholar 

  50. Lowdens, J. M., Hokin-Neaverson, M., and Bertics, P. J. (1990) Biochim. Biophys. Acta, 1052, 143–151.

    Google Scholar 

  51. Feschenko, M. S., and Sweadner, K. J. (1995) J. Biol. Chem., 270, 14072–14077.

    Google Scholar 

  52. Feschenko, M. S., and Sweadner, K. J. (1997) J. Biol. Chem., 272, 17726–17733.

    Google Scholar 

  53. Chibalin, A. V., Ogimoto, G., Pedemonte, C. H., Pressley, T., Katz, A., Feraile, Berggren, P.-O., and Bertorello, A. M. (1999) J. Biol. Chem., 274, 1920–1927.

    Google Scholar 

  54. Efendiev, R., Bertorello, A. M., Pressley, T., Rousselot, M., Feraile, E., and Pedemonte, C. H. (2000) Biochemistry, 39, 9884–9892.

    Google Scholar 

  55. Yudowski, G. A., Efendiev, R., Pedemonte, C. H., Katz, A., Berggren, P.-J., and Bertorello, A. (2000) Proc. Natl. Acad. Sci. USA, 97, 6556–6561.

    Google Scholar 

  56. Feraille, E., Carranza, M. L., Gonin, S., Beguin, P., Pedemonte, C., Rousselot, M., Caverzasio, J., Geering, K., Martin, P. V., and Favre, H. (1999) Mol. Biol. Cell, 10, 2847–2859.

    Google Scholar 

  57. Murtazina, D. A., Petukhov, S. P., Storey, K. B., Rubtsov, A. M., and Lopina, O. D. (1999) Biosci. Rep., 19, 109–114.

    Google Scholar 

  58. Blanko, G., Sanchez, G., and Mercer, R. (1998) Arch. Biochem. Biophys., 359, 139–150.

    Google Scholar 

  59. Lopina, O. D., Sarvazyan, N. A., Askari, A., and Boldyrev, A. (1995) Arch. Biochem. Biophys., 321, 429–433.

    Google Scholar 

  60. Martin, D. W., and Sachs, J. R. (1999) Biochemistry, 38, 7485–7497.

    Google Scholar 

  61. Boldyrev, A. A., Lopina, O. D., Kenny, M., and Johnson, P. (1995) Biochem. Biophys. Res. Commun., 216, 1048–1053.

    Google Scholar 

  62. Hopkins, B. E., Wagner, H., and Smith, T. (1976) J. Biol. Chem., 251, 4365–4371.

    Google Scholar 

  63. Lingham, R. B., Stewart, D. J., and Sen, A. K. (1980) Biochim. Biophys. Acta, 601, 229–234.

    Google Scholar 

  64. Pawson, T. (1995) Nature, 373, 573–580.

    Google Scholar 

  65. Blanko, G., and Mercer, R. W. (1995) Biochemistry, 34, 319–325.

    Google Scholar 

  66. Jasser, F., Canessa, C. M., Horisberger, J. D., and Rossier, B. (1992) J. Biol. Chem., 267, 16895–16903.

    Google Scholar 

  67. Lutsenko, S., and Kaplan, J. H. (1992) Ann. N. Y. Acad. Sci. USA, 671, 147–155.

    Google Scholar 

  68. Vladimirova, N. M., Murav.eva, T. I., Ovchinnikova, T. V., Potapenko, N. A., and Khodova, O. M. (1998) Biol. Membr. (Moscow), 15, 349–352.

    Google Scholar 

  69. Gloor, S., Stonicek, H., Sweadner, K. J., Pagliusi, S., Frank, R., Moos, M., and Schachner, M. (1990) J. Cell. Biol., 110, 165–174.

    Google Scholar 

  70. Swann, A. C. (1975) Biochim. Biophys. Acta, 401, 299–306.

    Google Scholar 

  71. Ochieng, J., Warfield, P., Green-Jarvis, B., and Fentie, I. (1999) J. Cell. Biochem., 75, 505–514.

    Google Scholar 

  72. Arystarkhova, E., Wetzel, R., Asinovski, N. K., and Sweadner, K. J. (1999) J. Biol. Chem., 274, 33183–33185.

    Google Scholar 

  73. Forbush, B., Kaplan, J. H., and Hoffman, J. F. (1978) Biochemistry, 17, 3667–3676.

    Google Scholar 

  74. Minor, N. T., Sha, Q., Nichols, C. G., and Mercer, R. W. (1998) Proc. Natl. Acad. Sci. USA, 95, 6521–6525.

    Google Scholar 

  75. Kuster, B., Shainskaya, A., Pu, H. X., Goldshleger, R., Blostein, R., Mann, M., and Karlish, S. J. (2000) J. Biol. Chem., 275, 18441–18446.

    Google Scholar 

  76. Mahmmoud, Y. A., Vorum, H., and Cornelius, F. (2000) J. Biol. Chem., 275, 35969–35977.

    Google Scholar 

  77. Rubtsov, A. M., and Lopina, O. D. (2000) FEBS Lett., 482, 1–5.

    Google Scholar 

  78. Devarajan, P., Scaramuzzino, and Morrow, J. S. (1994) Proc. Natl. Acad. Sci. USA, 91, 2965–2969.

    Google Scholar 

  79. Gorina, S., and Pavlevich, N. P. (1996) Science, 274, 1001–1005.

    Google Scholar 

  80. Marrs, J. A., Napolitano, E. W., Murphy-Erdos, C., Mays, R. W., Reichardt, and Nelson, W. J. (1993) J. Cell. Biol., 123, 149–164.

    Google Scholar 

  81. Alper, S. I., Stuart-Tilley, A., Simmons, C. F., Brown, D., and Drenckhalhn, D. (1994) J. Clin. Invest., 93, 1430–1438.

    Google Scholar 

  82. Gundersen, D., Orlovski, J., and Rodriguez-Boulan, E. (1991) J. Cell. Biol., 112, 863–872.

    Google Scholar 

  83. Gundersen, D., Powell, S. K., and Rodriguez-Boulan, E. (1993) J. Cell. Biol., 121, 335–343.

    Google Scholar 

  84. Nelson, W. J., and Hammerton, R. W. J. (1989) J. Cell. Biol., 108, 893–902.

    Google Scholar 

  85. Dubreuil, R. R., Maddux, P. B., Grushko, T. A., and MacVicar, G. R. (1997) Mol. Biol. Cell, 8, 1933–1942.

    Google Scholar 

  86. Van Dort, H. M., Moriyama, R., and Low, P. S. (1998) J. Biol. Chem., 273, 14819–14826.

    Google Scholar 

  87. Kataoka, M., Head, J. F., Seaton, B. A., and Engelman, D. M. (1989) Proc. Natl. Acad. Sci. USA, 86, 6944–6948.

    Google Scholar 

  88. He, Z., Dunker, A. K., Wesson, C. R., and Trumble, W. R. (1993) J. Biol. Chem., 268, 24635–24641.

    Google Scholar 

  89. Malencik, D. A., and Anderson, S. R. (1988) Biochemistry, 27, 1941–1949.

    Google Scholar 

  90. Fletcher, J. F., and Jang, M. S. (1993) Toxicon, 31, 669–695.

    Google Scholar 

  91. Voss, J., Birmachu, W., Hussey, D. M., and Thomas, D. D. (1991) Biochemistry, 30, 7498–7506.

    Google Scholar 

  92. Murtazina, D. A., Mast, N. V., Rubtsov, A. M., and Lopina, O. D. (1992) Biokhimiya, 67, 54–61.

    Google Scholar 

  93. Cuppoletti, J., Blumenthal, K. E., and Malinowska, D. H. (1989) Arch. Biochem. Biophys., 283, 249–257.

    Google Scholar 

  94. Birmachu, W., and Thomas, D. D. (1990) Biochemistry, 29, 3904–3914.

    Google Scholar 

  95. Shorina, E. A., Mast, N. V., Rubtsov, A. M., and Lopina, O. D. (1997) Biochemistry, 36, 13455–13460.

    Google Scholar 

  96. Cuppoletti, J., and Malinowska, D. H. (1992) Mol. Cell. Biochem., 114, 57–63.

    Google Scholar 

  97. Cuppoletti, J., and Abbot, A. (1990) Arch. Biochem. Biophys., 278, 405–415.

    Google Scholar 

  98. Cuppoletti, J., Blumenthal, K. E., and Malinowska, D. H. (1996) Arch. Biochem. Biophys., 278, 263–270.

    Google Scholar 

  99. Clarke, M., Conway, T. M., Shorr, R. G., and Crooke, S. T. (1987) J. Biol. Chem., 262, 4402–4406.

    Google Scholar 

  100. Peitsch, M. C., Borner, and Tschopp, J. (1993) TIBS, 18, 292–293.

    Google Scholar 

  101. Cuppoletti, J., Huang, P., Kaetzel, M. A., and Malinowska, D. H. (1993) Am. J. Physiol., 264, G637-G644.

    Google Scholar 

  102. Cuppoletti, J., Rubtsov, A. M., Behbehani, G., and Lopina, O. D. (1995) Biophys. J., 68, A235.

    Google Scholar 

  103. Lingrel, J. B., van Huysse, J., O.Brien, W., Jewell-Motz, E., Askew, R., and Schultheis, P. (1994) Kidney Int., 45, S32-S39.

    Google Scholar 

  104. Doris, P. (1994) PSEBM, 205, 202–212.

    Google Scholar 

  105. Buckalew, V. M., Jr., and Gonick, H. C. (1998) Clin. Exp. Hypertens., 20, 481–488.

    Google Scholar 

  106. Rogaeva, E. A., Perova, N. V., Alexandrov, A. A., Oganov, R. G., Lopina, O. D., and Boldyrev, A. A. (1987) Vopr. Med. Khim., 4, 34–39.

    Google Scholar 

  107. Haddy, F. J. (1984) J. Cardiovasc. Pharmacol., 6, S439-S456.

    Google Scholar 

  108. Tao, Q.-F., Hollenberg, N. K., and Graves, S. W. (1999) Hypertension, 34, 1168–1174.

    Google Scholar 

  109. Nakagawa, Y., Rivera, V., and Larner, A. C. (1992) J. Biol. Chem., 267, 8785–8788.

    Google Scholar 

  110. Peng, M., Huang, L., Xie, Z., Huang, W.-H., and Askari, A. (1996) J. Biol. Chem., 271, 10372–10378.

    Google Scholar 

  111. Kometiani, P., Li, J., Gnudi, L., Kahn, B., Askari, A., and Xie, Z. (1998) J. Biol. Chem., 273, 15249–15256.

    Google Scholar 

  112. Xie, Z., Kometiani, P., Liu, J., Li, J., Shapiro, J. I., and Askari, A. (1999) J. Biol. Chem., 274, 19323–19328.

    Google Scholar 

  113. Haas, M., Askari, A., and Xie, Z. (2000) J. Biol. Chem., 275, 27832–27837.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119899, Russia

    O. D. Lopina

Authors
  1. O. D. Lopina
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lopina, O.D. Interaction of Na,K-ATPase Catalytic Subunit with Cellular Proteins and Other Endogenous Regulators. Biochemistry (Moscow) 66, 1122–1131 (2001). https://doi.org/10.1023/A:1012432913689

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1012432913689

Search

Navigation