Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Ankyrin binding to (Na+ + K+)ATPase and implications for the organization of membrane domains in polarized cells

Nature volume 328, pages 533–536 (1987)Cite this article

Abstract

The interaction between membrane proteins and cytoplasmic structural proteins is thought to be one mechanism for maintaining the spatial order of proteins within functional domains on the plasma membrane1–4. Such interactions have been characterized extensively in the human erythrocyte5–7, where a dense, cytoplasmic matrix of proteins comprised mainly of spectrin and actin8, is attached through a linker protein, ankyrin, to the anion transporter (Band 3) 9,10. In several nonerythroid cell types, including neurons11–13, exocrine cells14 and polarized epithelial cells15,16 homologues of ankyrin and spectrin (fodrin) 11,12,15,17–23 are localized in specific membrane domains. Although these results suggest a functional linkage between ankyrin and fodrin and integral membrane proteins in the maintenance of membrane domains in nonerythroid cells, there has been little direct evidence of specific molecular interactions. Using a direct biological and chemical approach, we show here that ankyrin binds to the ubiquitous (Na+ + K+)ATPase, which has an asymmetrical distribution in polarized cells14, 24–30.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. 1. Singer, S. J. A. Rev. Biochem. 43, 805–833 (1974). 2. Nicolson, G. L. Biochim. Biophys. Acta 457, 57–108 (1974). 3. Edelman, G. M. Science 192, 218–226 (1976). 4. Bourguignon, L. Y. W. & Singer, S. J. Proc. natn. Acad. Sci. U.S.A. 74, 5031–5035 (1977). 5. Bennett, V. A. Rev. Biochem. 54, 273–304 (1985). 6. Branton, D., Cohen, C. M. & Tyler, J. Cell 24, 24–32 (1981). 7. Cohen, C. M. Semin. Hemat. 20, 141–158 (1983). 8. Lux, S. E., John, K. M. & Karnovsky, M. J. J. din. Invest. 58, 955–963 (1976). 9. Tyler, J. Hargreaves, W. & Branton, D. / biol Chem. 255, 7034–7039 (1979). 10. Bennett, V. & Stenbuck, P. J. biol. Chem. 255, 2540–2548 (1980). 11. Nelson, W. J. & Lazarides, E. Cell 39, 309–320 (1984). 12. Riederer, B. M., Zagon, I. S. & Goodman, S. R. / Cell Biol. 102, 2088–2097 (1986). 13. Lazarides, E. & Nelson, W. J. Science 220, 1295–1296 (1983). 14. Perrin, D. & Auris, D. Nature 315, 589–592 (1985). 15. Drenckhahn, D., Schluter, K., Alien, D. & Bennett, V. Science 230, 1287–1289 (1985). 16. Nelson, W. J. & Veshnock, P. J. J. Cell Biol. 103, 1751–1765 (1986). 17. Bennett, V., Baines, A. J. & Davis, J. Q. /. cell. Biochem. 29, 157–169 (1985). 18. Burridge, K., Kelley, T. & Mangeat, P. J. Cell. Biol. 95, 478–486. 19. Glenney, J. R. & Glenney, P. Cell 34, 503–512 (1983). 20. Bennett, V., Davis, J. & Fowler, W. A. Nature 299, 126–131 (1982). 21. Kay, M., Tracey, C., Goodman, J., Cone, J. & Bassel, P. Proc. natn. Acad. Sci. U.S.A. 80, 6882–6886 (1983). 22. Cox, J. V., Moon, R. T. & Lazarides, E. J. Cell Biol. 100, 1548–1557 (1985). 23. Nelson, W. J. & Lazarides, E. In Cell Membranes Methods and Reviews (eds E. Elson, W. Frazier & L. Glaser), 2, 219–246 (1984). 24. Vorbrodt, A., Konwinski, M., Solter, D. & Koprowski, H. Devl Biol. 55, 117–134 (1977). 25. Wiley, L. M. & Eglitis, M. A. Devl Biol. 86, 493–501 (1981). 26. Fleming, T. P. Bioassays 4, 105–109 (1986). 27. Glynn, I. M. & Karlish, S. J. D. A. Rev. Physiol. 37, 13–85 (1975). 28. Hobbs, A. S. & Albers, R. W. A. Rev. Biophys. Bioengng 9, 259–291 (1980). 29. Hesketh, J. E. Cell Biol. Int. Rep. 10, 85–89 (1986). 30. Hootman, S. R. Int. Rev. Cytol. 105, 129–181 (1986). 31. J0rgensen, P. L. Biochim. Biophys. Acta 694, 27–68 (1982). 32. Karlish, S. J. D. & Yates, D. W. Biochim. Biophys. Acta 527, 115–130 (1978). 33. Giotta, G. J. biol. Chem. 250, 5159–5164 (1975). 34. Brotherus, J. R., M011er, J. V. & J0rgensen, P. L. Biochem. biophys. Res. Commun. 100, 146–154 (1981). 35. Georgatas, S. D., & Marchesi, V. T. /. Cell Biol. 100, 1955–1961 (1985). 36. Davis, J. Q. & Bennett, V. J. biol. Chem. 259, 13550–13559 (1984). 37. Matlin, K. S. & Simons, K. J. Cell Biol. 99, 2131–2139 (1984). 38. Misek, D. E., Bard, E. & Rodriguez–Boulan, E. Cell 59, 537–546 (1984). 39. Pfeiffer, S., Fuller, S. D. & Simons, K. / Cell Biol. 101, 470–476 (1985). 40. Rindler, M. J., Ivanov, I. E., Plesken, H. & Sabatini, D. D. /. Cell Biol. 100, 136–151 (1985). 41. Rodriguez–Boulan, E. Mod. Cell Biol. 1, 119–170 (1983). 42. Simons, K. & Fuller, S. D. A. Rev. Cell Biol. 1, 243–288 (1985). 43. Gonzalez–Mariscal, L., Chavez de Ramirez, B. & Cereijido, M. /. membr. Biol. 86, 113–125 (1985). 44. Pasaur, M. & Ripoche, P. J. Cell Biol. 71, 907–920 (1976). 45. Van Meer, G. & Simons, K. EMBO J. 5, 1455–1464 (1986). 46. Louvard, D. Proc. natn. Acad. Sci. U.S.A. 77, 4132–4136 (1980). 47. Caplan, M. J., Anderson, M. C., Palade, G. E. & Jamieson, J. D. Cell 46, 623–631 (1986). 48. Nelson, W. J. & Veshnock, P. J. /. Cell Biol. 104, 1527–1537 (1987). 49. Laemlli, V. K. Nature 227, 680–685 (1970). 50. Bennett, V. Meth. Enzym. 96, 313–324 (1983). 51. Castro, J. & Parley, R. A. J. biol. Chem. 254, 2221–2228 (1979). 52. Morrow, J. S. & Haigh, W. B. Meth. Enzym. 96, 298–304 (1983). 53. Oakley, B. R., Kirsch, D. B. & Morris, N. R. Analyt. Biochem. 105, 361–363 (1980).

Download references

Author information

Authors and Affiliations

  1. Institute for Cancer Research, 7701 Burholme Avenue, Philadelphia, Pennsylvannia, 19111, USA

    W. James Nelson & Pamela J. Veshnock

Authors
  1. W. James Nelson
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Pamela J. Veshnock
    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

Nelson, W., Veshnock, P. Ankyrin binding to (Na+ + K+)ATPase and implications for the organization of membrane domains in polarized cells. Nature 328, 533–536 (1987). https://doi.org/10.1038/328533a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/328533a0

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.

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing