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Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide

Nature volume 318, pages 295–298 (1985)Cite this article

Abstract

Many of the physical properties of the erythrocyte membrane appear to depend on the membrane skeleton, which is attached to the membrane through associations with transmembrane proteins1–5. A membrane skeletal protein, protein 4.1, is pivotal in the assembly of the membrane skeleton because of its ability to promote associations between spectrin and actin5–9. Protein 4.1 also binds to the membrane through at least two sites: a high-affinity site on the glycophorins2,10 and a site of lower affinity associated with band 3 (ref. 11). The glycophorin–protein 4.1 association has been proposed to be involved in maintenance of cell shape2,12,13. Here we show that the association between glycophorin and protein 4.1 is regulated by a polyphosphoinositide cofactor. This observation suggests a mechanism which may explain the recently reported dependence of red cell shape on the level of polyphosphoinositides in the membrane14–16.

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References

  1. Bennett, V & Stenbuck, P. J. Nature 280, 468–473 (1979); J. biol. Chem. 255, 2540–2548 (1980).

    Article  ADS  CAS  Google Scholar 

  2. Anderson, R.A. & Lovrien, R.E. Nature 307, 655–658 (1984).

    Article  ADS  CAS  Google Scholar 

  3. Sheetz, M.P. & Singer, S.J. J. Cell Biol. 73, 638–646 (1977).

    Article  CAS  Google Scholar 

  4. Nicolson, G.L. & Painter, R.G. J. Cell Biol. 59, 395–406 (1973).

    Article  CAS  Google Scholar 

  5. Tyler, J.M., Reinhardt, B.N. & Branton, D. J. biol. Chem. 255, 7034–7039 (1980).

    CAS  PubMed  Google Scholar 

  6. Ungewickell, E., Bennet, P.M., Calvert, R., Ohanian, V. & Gratzer, W.B. Nature 280, 811–814 (1979).

    Article  ADS  CAS  Google Scholar 

  7. Fowler, V. & Taylor, D.L. J. Cell Biol. 85, 361–376 (1980).

    Article  CAS  Google Scholar 

  8. Cohen, C.M. & Foley, S.F. Biochim. biophys. Acta 688, 691–701 (1982).

    Article  CAS  Google Scholar 

  9. Ohanian, U. et al. Biochemistry 23, 4416–4420 (1984).

    Article  CAS  Google Scholar 

  10. Mueller, T.J. & Morrison, M. Erythrocyte Membranes Vol. 2, 95–112 (Liss, New York, 1981).

    Google Scholar 

  11. Pasternack, G.R., Anderson, R.A., Leto, T. & Marchesi, V.T. J. Biol. Chem. 260, 3676–3683 (1985).

    CAS  PubMed  Google Scholar 

  12. Anderson, R.A. & Lovrien, R.E. Nature 292, 158–161 (1981).

    Article  ADS  CAS  Google Scholar 

  13. Chasis, J.A., Mohandas, N., Mentzer, W., Walker, P. & Shohet, S.B. Blood, 25 (1983).

  14. Michell, R.H. Biochim. biophys. Acta 415, 81–147 (1975).

    Article  CAS  Google Scholar 

  15. Ferrell, J.E. & Huestis, W.H. J. Cell Biol. 98, 1992–1998 (1984).

    Article  CAS  Google Scholar 

  16. Allan, D. & Thomas, P. Biochem. J. 198, 433–440 (1981).

    Article  CAS  Google Scholar 

  17. Furthmayr, H. & Marchesi, V.T. Meth. Enzym. 96, 268–280 (1983).

    Article  CAS  Google Scholar 

  18. Marchesi, V.T. & Andrews, E.P. Science 174, 1247–1249 (1971).

    Article  ADS  CAS  Google Scholar 

  19. Van Zoelen, E.J.J., Zwaal, R.F.A., Reuvers, F.A.M., Demel, R.A. & Van Deenen, L.L.M. Biochim. biophys. Acta 464, 482–492 (1977).

    Article  CAS  Google Scholar 

  20. Buckley, J.T., J. Biochem. 56, 349–351 (1978).

    CAS  Google Scholar 

  21. Shukla, H.D., Colemen, R., Finean, J.B. & Michell, R.H. Biochem. J. 179, 441–444 (1979).

    Article  CAS  Google Scholar 

  22. Armitage, I.M., Shapiro, D.L., Furthmayr, H. & Marchesi, V.T. Biochemistry 16, 1317–1320 (1977).

    Article  CAS  Google Scholar 

  23. Speicher, D.W., Morrow, J.S., Knowles, W.J. & Marchesi, V.T. J. Biol. Chem. 257, 9093–9101 (1982).

    CAS  PubMed  Google Scholar 

  24. Tyler, J.M., Hargreaves, W. & Branton, D. Proc. natn. Acad. Sci. U.S.A. 76, 5192–5196 (1979).

    Article  ADS  CAS  Google Scholar 

  25. Hargreaves, W.R., Giedd, K.N., Verkleij, A. & Branton, D. J. Biol, Chem. 255, 11965–11972 (1980).

    CAS  Google Scholar 

  26. Dixon, M. Biochem. J. 55, 170–171 (1953).

    Article  CAS  Google Scholar 

  27. Mimms, L.T., Zampighi, G., Nozaki, Y., Tanford, C. & Reynolds, J.A. Biochemistry 20, 833–840 (1981).

    Article  CAS  Google Scholar 

  28. Sato, S.B. & Onnishi, S., Eur, J. Biochem. 130, 19–26 (1983).

    CAS  Google Scholar 

  29. Berridge, M.J. & Irvine, R.F. Nature 312, 315–321 (1984).

    Article  ADS  CAS  Google Scholar 

  30. Downes, C.P. & Michell, R.H. Cell Calcium 3, 467–502 (1982).

    Article  CAS  Google Scholar 

  31. Irvine, R.F. Cell Calcium 3, 295–309 (1982).

    Article  CAS  Google Scholar 

  32. Allan, D. & Michell, R.H. Biochim. biophys. Acta 508, 277–286 (1978).

    Article  CAS  Google Scholar 

  33. Downes, C.P. & Mitchell, R.H. Biochem. J. 198, 133–140 (1981).

    Article  CAS  Google Scholar 

  34. Allan, D., Thomas, P. & Michell, R.H. Nature 276, 289–290 (1978).

    Article  ADS  CAS  Google Scholar 

  35. Sheetz, M.P. & Singer, S.J. Proc. natl. Acad. Sci. U.S.A. 71, 4457–4461 (1974).

    Article  ADS  CAS  Google Scholar 

  36. Berridge, M.J. Biochem. J. 220, 345–360 (1984).

    Article  CAS  Google Scholar 

  37. Majerus, P.W., Neufeld, E.J. & Wilson, D.B. Cell 37, 701–703 (1984).

    Article  CAS  Google Scholar 

  38. Nishizuka, Y. Nature 308, 693–698 (1984).

    Article  ADS  CAS  Google Scholar 

  39. Cohen, C.M., Foley, S.F. & Korsgren, C. Nature 299, 648–650 (1982).

    Article  ADS  CAS  Google Scholar 

  40. Spiegel, J.E., Beardsley, D.S., Southwick, F.S. & Lux, S.E. J. Cell Biol. 99, 886–893 (1984).

    Article  CAS  Google Scholar 

  41. Goodman, S.R., Casoria, L.A., Coleman, D.B. & Zagon, I.G. Science 224, 1433–1438 (1984).

    Article  ADS  CAS  Google Scholar 

  42. Granger, B.L. & Lazarides, E. Cell 37, 595–607 (1984).

    Article  CAS  Google Scholar 

  43. Aster, J.C., Welsh, M.J., Brewer, G.J. & Maisel, H. Biochem. biophys. Res. Commun. 119, 226–234 (1984).

    Article  Google Scholar 

  44. Granger, B.L. & Lazarides, E. Nature 313, 238–241 (1985).

    Article  ADS  CAS  Google Scholar 

  45. Baines, A.J. & Bennett, V. Nature 315, 410–413 (1985).

    Article  ADS  CAS  Google Scholar 

  46. Leto, T.L., Pratt, B.M. & Madri, J. Fedn. Proc. 44, 1600 (1985).

    Google Scholar 

  47. Navone, F., Greengard, P. & DeCamilli, P. Science 226, 1209–1211 (1985).

    Article  ADS  Google Scholar 

  48. DeCamilli, P., Cameron, R. & Greengard, P. J. Cell Biol. 96, 1337–1354 (1983).

    Article  CAS  Google Scholar 

  49. Bartlett, G.R. J. Biol. Chem. 234, 466–468 (1969).

    Google Scholar 

  50. Duck-chong, C.G. Lipids 14, 492–497 (1979).

    Article  CAS  Google Scholar 

  51. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. J. Biol. Chem. 193, 265–275 (1951).

    CAS  Google Scholar 

  52. Leto, T.L. & Marchesi, V.T. J.Biol. Chem. 259, 4603–4608 (1984).

    CAS  PubMed  Google Scholar 

  53. Sacht, J. J. Lipid Res. 19, 1063–1067 (1978).

    Google Scholar 

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Authors and Affiliations

  1. Department of Pathology, Yale University School of Medicine, 310 Cedar Street, PO Box 3333, New Haven, Connecticut, 06510, USA

    Richard A. Anderson & Vincent T. Marchesi

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  1. Richard A. Anderson
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  2. Vincent T. Marchesi
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Anderson, R., Marchesi, V. Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide. Nature 318, 295–298 (1985). https://doi.org/10.1038/318295a0

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