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Sequence and domain structure of talin

Abstract

TALIN is a high-molecular-weight cytoskeletal protein concentrated at regions of cell–substratum contact1 and, in lymphocytes, at cell–cell contacts2,3. Integrin receptors are involved in the attachment of adherent cells to extracellular matrices4,5 and of lymphocytes to other cells6. In these situations, talin codistributes with concentrations of integrins in the cell surface membrane3,7–9. Furthermore, in vitro binding studies suggest that integrins bind to talin, although with low affinity10. Talin also binds with high affinity to vinculin11, another cytoskeletal protein concentrated at points of cell adhesion12. Finally, talin is a substrate for the Ca2+-activated protease, calpain II13,14, which is also concentrated at points of cell-substratum contact14. To learn more about the structure of talin and its involvement in transmembrane connections between extracellular adhesions and the cytoskeleton, we have cloned and sequenced murine talin. We describe a model for the structure of talin based on this sequence and other data. Homologies between talin and other proteins define a novel family of submembranous cytoskeleton-associated proteins all apparently involved in connections to the plasma membrane.

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References

  1. Burridge, K. & Connell, L. J. Cell Biol. 97, 359–367 (1983).

    Article  CAS  PubMed  Google Scholar 

  2. Kupfer, A., Singer, S. J. & Dennert, G. J. exp. Med. 163, 489–498 (1986).

    Article  CAS  PubMed  Google Scholar 

  3. Burn, P., Kupfer, A. & Singer, S. J. Proc. natn. Acad. Sci. U.S.A. 85, 497–501 (1988).

    Article  ADS  CAS  Google Scholar 

  4. Hynes, R. O. Cell 48, 549–554 (1987).

    Article  CAS  PubMed  Google Scholar 

  5. Ruoslahti, E. & Pierschbacher, M. D. Science 238, 491–497 (1987).

    Article  ADS  CAS  PubMed  Google Scholar 

  6. Anderson, D. C. & Springer, T. A. A. Rev. Med 38, 175–194 (1987).

    Article  CAS  Google Scholar 

  7. Chen, W, T., Hasegawa, T., Hasegawa, C., Weinstock, C. & Yamada, K. M. J. Cell Biol. 100, 1103–1114 (1985).

    Article  CAS  PubMed  Google Scholar 

  8. Damsky, C. M., Knudsen, K. A., Bradley, D., Buck, C. A. & Horwitz, A. J. Cell Biol. 100, 1528–1539 (1985).

    Article  CAS  PubMed  Google Scholar 

  9. Kupfer, A. & Singer, S. J. J. exp. Med. 170, 1697–1713 (1989).

    Article  CAS  PubMed  Google Scholar 

  10. Horwitz, A., Duggan, E., Buck, C., Beckerle, M. C. & Burridge, K. Nature 320, 531–533 (1986).

    Article  ADS  CAS  PubMed  Google Scholar 

  11. Burridge, K. & Mangeat, P. Nature 308, 744–746 (1984).

    Article  ADS  CAS  PubMed  Google Scholar 

  12. Geiger, B. Cell 18, 193–205 (1979).

    Article  CAS  PubMed  Google Scholar 

  13. Fox, J. E. B., Goll, D. E., Reynolds, C. C. & Phillips, D. R. J. biol. Chem. 260, 1060–1066 (1985).

    CAS  PubMed  Google Scholar 

  14. Beckerle, M. C., Burridge, K., DeMartino, G. N. & Croall, D. E. Cell 51, 569–577 (1987).

    Article  CAS  PubMed  Google Scholar 

  15. Kozak, M. Nucleic Acids Res. 12, 857–872 (1984).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  16. Molony, L., McCaslin, D., Abernethy, J., Paschal, B. & Burridge, K. J. biol. Chem. 262, 7790–7795 (1987).

    CAS  PubMed  Google Scholar 

  17. Akrigg, D. et al. Nature 335, 745–746 (1988).

    Article  Google Scholar 

  18. Bennett, V. A. Rev. Biochem. 54, 273–304 (1985).

    Article  CAS  Google Scholar 

  19. Marchesi, V. T. A. Rev. Cell Biol. 1, 531–561 (1985).

    Article  CAS  Google Scholar 

  20. Bretscher, A. Meth. Eznym. 134, 24–37 (1986).

    CAS  Google Scholar 

  21. Pakkanen, R., Hedman, K., Turunen, O., Wahlstrom, T. & Vaheri, A. J. Histochem. Cytochem. 35, 809–816 (1987).

    Article  CAS  PubMed  Google Scholar 

  22. Turunen, O. et al. J. biol. Chem. 264, 16727–16732 (1989).

    CAS  PubMed  Google Scholar 

  23. Gould, K. L., Cooper, J. A., Bretscher, A. & Hunter, T. J. Cell Biol. 102, 660–669 (1986).

    Article  CAS  PubMed  Google Scholar 

  24. Gould, K. L., Bretscher, A., Esch, F. S. & Hunter, T. EMBO J. 8, 4133–4142 (1989).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  25. Bretscher, A. J. Cell Biol. 97, 425–432 (1983).

    Article  CAS  PubMed  Google Scholar 

  26. Pakkanen, R. J. cell. Biochem. 38, 65–75 (1988).

    Article  CAS  PubMed  Google Scholar 

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

    Article  ADS  CAS  PubMed  Google Scholar 

  28. Anderson, R. A. & Marchesi, V. T. Nature 318, 295–298 (1985).

    Article  ADS  CAS  PubMed  Google Scholar 

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

    CAS  PubMed  Google Scholar 

  30. Leto, T. L., Correas, I., Tobe, T., Anderson, R. A. & Horne, W. C. in Membrane Skeletons and Cytoskeletal Membrane Associations (eds Bennett, V., Cohen, C. M., Lux, S. E. & Palek, J.) 201–209 (Liss, New York, 1986).

    Google Scholar 

  31. Birgbauer, E. & Solomon, F. J. Cell Biol. 109, 1609–1620 (1989).

    Article  CAS  PubMed  Google Scholar 

  32. Goslin, K., Birgbauer, E., Banker, G. & Solomon, F. J. Cell Biol. 109, 1621–1631 (1989).

    Article  CAS  PubMed  Google Scholar 

  33. Conboy, J., Kan, Y. W., Shohet, S. B. & Mohandas, N. Proc. natn. Acad. Sci. U.S.A. 83, 9512–9516 (1986).

    Article  ADS  CAS  Google Scholar 

  34. Rogers, S., Wells, R., & Rechsteiner, M. Science 234, 364–368 (1986).

    Article  ADS  CAS  PubMed  Google Scholar 

  35. Wang, K. K. W., Villalobo, A. & Roufogalis, B. D. Biochem. J. 262, 693–706 (1989).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  36. Staden, R. Meth. Enzym. 183, 163–180 (1990).

    Article  CAS  PubMed  Google Scholar 

  37. Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).

    Article  ADS  CAS  Google Scholar 

  38. Tabor, S. & Richardson, C. C. Proc. natn. Acad. Sci. U.S.A. 84, 4767–4771 (1987).

    Article  ADS  CAS  Google Scholar 

  39. DeMartino, G. N. & Croall, D. E. Biochemistry 22, 6287–6291 (1983).

    Article  CAS  PubMed  Google Scholar 

  40. Matsudaira, P. J. biol. Chem. 262, 10035–10038 (1987).

    CAS  PubMed  Google Scholar 

  41. Tang, T. K. et al. Proc. natn. Acad. Sci. U.S.A. 85, 3713–3717 (1988).

    Article  ADS  CAS  Google Scholar 

  42. Giebelhaus, D. H., Eib, D. W. & Moon, R. T. Cell 53, 601–615 (1988).

    Article  CAS  PubMed  Google Scholar 

  43. Tang, T. K., Qin, Z., Leto, T., Marchesi, V. T. & Benz, E. J. Jr J. Cell Biol. 110, 617–624 (1990).

    Article  CAS  PubMed  Google Scholar 

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Rees, D., Ades, S., Singer, S. et al. Sequence and domain structure of talin. Nature 347, 685–689 (1990). https://doi.org/10.1038/347685a0

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