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:

Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases

Nature volume 355, pages 78–80 (1992)Cite this article

Abstract

THE high-affinity IgE receptor (FcɛRI), which is expressed on the surface of mast cells and basophils, has a central role in immediate allergic responses. In the rat basophilic leukaemia cell line RBL-2H3, which is a model system for the analysis of FcɛRI-mediated signal transduction, surface engagement of FcɛRI induces histamine release and the tyrosine phosphorylation of several distinct proteins1. Although the α, β and γ subunits of FcɛRI lack intrinsic tyrosine protein kinase (TPK) activity, a kinase that copurifies with FcɛRI phosphorylates the β and γ subunits of the receptor on tyrosine residues2,3. We report here that in RBL-2H3 cells, p56lyn and pp60c-src are activated after FcɛRI crosslinking, and p56lyn coimmunoprecipitates with FcɛRI. In the mouse mastcell line PT-18, another cell type used to study FCɛRI-mediated signalling, tyrosine phosphorylation of proteins is also an immediate consequence of receptor crosslinking. Notably, the only detectable src protein-related TPK in PT-18 cells is p62c-yes, and it is this TPK that is activated on FcɛRI engagement and coimmunoprecipitates with the receptor. Therefore, it seems that different src protein-related TPKs can associate with the same receptor and become activated after receptor engagement.

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. Benhamou, M., Gutkind, J. S., Robbins, K. C. & Siraganian, R. P. Proc. natn. Acad. Sci. U.S.A. 87, 5327–5330 (1990).

    Article  ADS  CAS  Google Scholar 

  2. Quarto, R. & Metzger, H. Molec. Immun. 23, 1215–1223 (1986).

    Article  CAS  Google Scholar 

  3. Shimuzu, A. et al. Proc. natn. Acad. Sci. U.S.A. 85, 1907–1911 (1988).

    Article  ADS  Google Scholar 

  4. Metzger, H. et al. A. Rev. Immun. 4, 419–470 (1986).

    Article  CAS  Google Scholar 

  5. Veillette, A., Bookman, M. A., Horak, E. M. & Bolen, J. B. Cell 55, 301–308 (1988).

    Article  CAS  Google Scholar 

  6. Rudd, C. E., Trevillyan, J. M., Dasgupta, J. D., Wong, L. L. & Schlossman, S. F. Proc. natn. Acad. Sci. U.S.A. 85, 5190–5194 (1988).

    Article  ADS  CAS  Google Scholar 

  7. Barber, E. K., Dasgupta, J. D., Schlossman, S. F., Trevillyan, J. M. & Rudd, C. E. Proc. natn. Acad. Sci. U.S.A. 86, 3277–3281 (1989).

    Article  ADS  CAS  Google Scholar 

  8. Samelson, L. E., Phillips, A. F., Loung, E. T. & Klausner, R. D. Proc. natn. Acad. Sci. U.S.A. 87, 4358–4362 (1990).

    Article  ADS  CAS  Google Scholar 

  9. Burkhardt, A. L., Brunswick, M., Bolen, J. B. & Mond, J. J. Proc. natn. Acad. Sci. U.S.A. 88, 7410–7414 (1991).

    Article  ADS  CAS  Google Scholar 

  10. Huang, M. M., Bolen, J. B., Barnwell, J. W., Shattil, S. J. & Brugge, J. S. Proc. natn. Acad. Sci. U.S.A. 88, 7844–7848 (1991).

    Article  ADS  CAS  Google Scholar 

  11. Yi, T., Bolen, J. B. & Ihle, J. N. Molec. cell. Biol. 11, 2391–2398 (1991).

    Article  CAS  Google Scholar 

  12. Hempstead, B. L., Parker, C. W. & Kulczycki, A. Jr J. biol. Chem. 256, 10717–10723 (1981).

    CAS  PubMed  Google Scholar 

  13. Holowka, D. & Baird, B. J. biol. Chem. 259, 3720–3728 (1984).

    CAS  PubMed  Google Scholar 

  14. Kulczycki, A. Jr & Parker, C. W. J. biol. Chem. 254, 3187–3193 (1979).

    CAS  PubMed  Google Scholar 

  15. Hempstead, B. L., Kulczycki, A. Jr & Parker, C. W. Biochem. biophys. Res. Commun. 98, 815–822 (1981).

    Article  CAS  Google Scholar 

  16. Holowka, D., Hartmann, H., Kanellopoulos, J. & Metzger, H. J. Receptor Res. 1, 41–68 (1980).

    Article  CAS  Google Scholar 

  17. Barsumian, E. L., Isersky, C., Petrino, M. G. & Siriganian, R. P. Eur. J. Immun. 11, 317–323 (1981).

    Article  CAS  Google Scholar 

  18. Lui, F.-T. et al. J. Immun. 124, 2728–2736 (1980).

    Google Scholar 

  19. Holowka, D. & Metzger, H. Molec. Immun. 19, 219–227 (1982).

    Article  CAS  Google Scholar 

  20. Basciano, L. K., Berenstein, E. H., Kmak, L. & Siriganian, R. P. J. biol. Chem. 261, 11823–11831 (1986).

    CAS  PubMed  Google Scholar 

  21. Baniyash, M., Alkalay, I. & Eshhar, Z. J. J. Immun. 138, 2999–3004 (1987).

    CAS  PubMed  Google Scholar 

  22. Lipsich, L. A., Lewis, A. J. & Brugge, J. S. J. Virol. 48, 352–360 (1983).

    CAS  PubMed  PubMed Central  Google Scholar 

  23. Bolen, J. B., Thompson, P. A., Eiseman, E. & Horak, I. D. Adv. Cancer Res. 57, 103–149 (1991).

    Article  CAS  Google Scholar 

  24. Rivera, J., Kinet, J.-P., Kim, J., Pucillo, C. & Metzger, H. Molec. Immun. 25, 647–661 (1988).

    Article  CAS  Google Scholar 

  25. Pluznik, D. H., Tare, N. S., Zatz, M. M. & Goldstein, A. L. Exp. Hemat. 10, 211–218 (1982).

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey, 08543-4000, USA

    Eiseman & Joseph B. Bolen

Authors
  1. Eiseman
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Joseph B. Bolen
    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

Eiseman, Bolen, J. Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature 355, 78–80 (1992). https://doi.org/10.1038/355078a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/355078a0

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