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.

  • Article
  • Published:

Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins

Nature volume 344, pages 36–42 (1990)Cite this article

Abstract

Analysis of complementary DNA for human erythroid ankyrin indicates that the mature protein contains 1,880 amino acids comprising an N-terminal domain binding integral membrane proteins and tubulin, a central domain binding spectrin and vimentin, and an acidic C-terminal 'regulatory' domain containing an alternatively spliced sequence missing from ankyrin variant 2.2. The N-terminal domain is almost entirely composed of 22 tandem 33-amino-acid repeats. Similar repeats are found in yeast and invertebrate proteins involved in cell-cycle control and tissue differentiation.

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. Bennett, V. & Branton, D. J. biol. Chem. 252, 2753–2763 (1977). 2. Bennett, V. & Stenbuck, P. J. J. biol. Chem. 254, 2533–2541 (1979). 8. Davis, J. Q. & Bennett, V. J. biol. Chem. 259, 1874–1881 (1984). 9. Bennett, V. & Davis, J. Proc. natn. Acad. Sci. U.S.A. 78, 7550–7554 (1981). 10. Bennett, V. Nature 281, 597–599 (1979). 11. Moon, R. T., Ngai, J, Wold, B. J. & Lazarides, E. J. Cell. Biol. 100,152–160 (1985). 12. Nelson, W. J. & Lazarides, E. Proc. natn. Acad. Sci. U.S.A. 81, 3292–3296 (1984). 13. Nelson, W. J. & Lazarides, E. Cell 39, 309–320 (1984). 14. Drenckhahn, D. & Bennett, V. Eur. J. Cell. Biol. 43, 479–486 (1987). 15. Alien, D. P., Low, P. S., Dola, A. & Maisel, H. Biochem. biophys. Res. Commun. 149,266–275 (1987). 16. Kalomiris, E. L & Bourguignon, L Y. W. J. Cell. Biol. 106, 319–327 (1988). 17. Davis, J., Davis, L. & Bennett, V. J. biol. Chem. 264, 6417–6426. (1989). 18. Koob, R., Zimmermann, M., Schoner, W. & Drenckhahn, D. Eur. J. Cell Biol. 45, 230–237 (1988). 19. Nelson, W. J. & Hammerton, R. W. J. Cell Biol. 108, 893–902 (1989). 20. Morrow, J. S., Cianci, C. D., Ardito, T., Mann, A. S. & Kashgarian, M. J. Cell Biol. 108,455–465 (1989). 21. Srinivasan, Y., Elmer, L, Davis, J., Bennett, V. & Angelides, K. Nature 333, 177–180 (1988). 22. Kordeli, E., Davis, J., Trapp, B. & Bennett, V. J. Cell Biol. (in the press). 23. Weaver, D. C., Pasternack, G. R. & Marchesi, V. T. J. biol. Chem. 259, 6165–6169 (1984). 24. Wallin, R., Gulp, E. N., Coleman, D. B. & Goodman, S. R. Proc. natn. Acad. Sei. U.S.A. 81, 4095–4099 (1984). 25. Davis, J. Q. & Bennett, V. J. biol Chem. 259, 13550–13559 (1984). 26. Weaver, D. C., Pasternack, G. R. & Marchesi, V. T. J. biol. Chem. 259, 6170–6175 (1984). 27. Bennett, V. J. biol. Chem. 253, 2292–2299 (1978). 28. Georgatos, S. D., Weaver, D. C. & Marchesi, V. T. J. Cell Biol. 100, 1962–1967 (1985). 29. Korsgren, C. & Cohen, C. N. J. biol. Chem. 263, 10212–10218 (1988). 30. Hall, T. G. & Bennett, V. J. biol. Chem. 262, 10537–10545 (1987). 31. Conboy, J., Kan, Y. W., Shohet, S. B. & Mohandas, N. Proc. natn. Acad. Sei. U.S.A. 83, 9512–9516 (1986). 32. Kozak, M. Nucleic Acids Res. 12, 857–871 (1984). 33. Boissel, J-P., Kasper, T. J., Shah, S. C., Malone, J. I. & Bunn, H. F. Proc. natn. Acad. Sei. U.S.A. 82, 8448–8452 (1985). 34. Lu, P-W., Soong, C–J. & Tão, M. J. biol. Chem. 260, 14958–14964 (1985). 35. Cianci, C. D, Giorgi, M. & Morrow, J. S. J. Cell Biochem. 37, 301–315 (1988). 36. Soong, C. J., Lu, P. W. & Tão, M. Archs Biochem. Biophys. 254, 509–517 (1987). 37. Boivin, P. & Garland, C. Biochem. biophys. ©s. Commun. 89, 7–16 (1979). 38. Rubin, C. S. J. biol. Chem. 254, 12439–12449 (1979). 39. Fairbanks, G. & Avruch, J. Biochemistry 13, 5514–5521 (1974). 40. Kuenzel, E. A., Mulligan, J. A., Summercorn, J. & Krebs, E. G. J. biol. Chem. 262,9136–9140 (1987). 41. Feramisco, J. R., Glass, D. B. & Krebs, E. G. J. biol. Chem. 255, 4240–4245 (1980). 42. Staufenbiel, M. & Lazarides, E. Proc. natn. Acad. Sei. U.S.A. 83, 318–322 (1986). 43. Staufenbiel, M. Molec. cell. Biol. 7, 2981–2984 (1987). 44. Mount, S. M. Nucleic Acids Res. 10, 459–472 (1982). 45. Wasenius, V-M. et ai. J. Cell Biol. 108, 79–93 (1989). 46. Wharton, K. A., Johansen, K. M., Xu, T. & Artavanis–Tsakonas, S. Cell 43, 567–581 (1985). 47. Yochem, J., Weston, K. & Greenwald, I. Nature 335, 547–550 (1988). 48. Yochem, J, & Greenwald, I. Cell 58, 553–563 (1989). 49. Artavanis-Tsakonas, S. Trends Genet. 4, 95–100 (1988). 50. Hartley, D. "., Xu, T. & Artavanis–Tsakonas, S. EMBO J. 6, 3407–3417 (1987). 51. Kidd, S., Baylies, M. K., Gasic, G. P. & Young, M. W. Genes Dei/. 3, 1113–1129 (1989). 52. Greenwald, l. S., Sternberg, P. W. & Horvitz, H. R. Cell 34, 435–444 (1983). 53. Sternberg, P. W. Nature 335, 551–554 (1988). 54. Sternberg, P. W. & Horvitz, H. R. Cell 58, 679–693 (1989). 55. Seydoux, G. & Greenwald, l. S. Cell 57, 1237–1245 (1989). 56. Austin, J. & Kimble, J. Cell 51, 589–599 (1987). 57. Hartley, D. "., Preiss, Z. & Artavanis–Tsakonas, S. Cell 55, 785–795 (1988). 58. Aves, S. J., Durkacz, B. W., Carr, A. & Nurse, P. EMBO J. 4, 457–463 (1985). 59. Breeden, L. & Nasmyth, K. Nature 329, 651–654 (1987). 60. Andrews, B. J. & Herskowitz, I. Nature 342, 830–833 (1989). 61. Nasmyth, K. & Shore, D. Science 237, 1162–1170, (1987). 62. Gillard, S., Spehner, D., Drillien, R. & Kirn, A. Proc. natn. Acad. Sei. U.S.A. 83, 5573–5577 (1986). 63. Spehner, D., Gillard, S., Drillien, R. & Kirn, A. J. Virol. 62, 1297–1304 (1988). 64. Davis, J. & Bennett, V. J. biol. Chem. 258, 7757–7766 (1983). 65. Young, R. A. & Davis, R. W. in Genetic Engineering Vol. 7 (eds Setlow, J. K. & Hollaender, A.) 29 (Plenum, New York, 1985). 66. Toneguzzo, F., Glynn, S., Levi, E., Mjolsness, S. & Hayday, A. BioTechniques 6, 460–469 (1988). 67. Henikoff S. Gene 28, 351–359 (1984). 68. Devereux, J., Haekerli, P. & Smithies, 0. Nucleic Acids Res. 12, 387–395 (1984). 69. Gribskov, M. & Burgess, R. R. Nucleic Acids Res. 14, 6745–6763 (1986). 70. Johansen, K. M., Fehon, R. G. & Artavanis-Tsakonas, S. J. Cell. Biol. 109, 2427–2440 (1989).

Download references

Author information

Authors and Affiliations

  1. Division of Hematology/Oncology, The Children's Hospital and Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts, 02115, USA

    Samuel E. Lux & Kathryn M. John

  2. Howard Hughes Medical Institute and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710, USA

    Vann Bennett

Authors
  1. Samuel E. Lux
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Kathryn M. John
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Vann Bennett
    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

Lux, S., John, K. & Bennett, V. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature 344, 36–42 (1990). https://doi.org/10.1038/344036a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/344036a0

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