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:

Association of folding intermediates of glycoproteins with calnexin during protein maturation

Abstract

Calnexin, an endoplasmic reticulum transmembrane protein, represents a new type of molecular chaperone that selectively associates in a transient fashion with newly synthesized monomeric glycoproteins in HepG2 cells. Calnexin only recognizes glycoproteins when they are incompletely folded. Dissociation of glycoproteins from calnexin occurs at different rates and is related to the time taken for their folding, which may then initiate their differential transport rates from the endoplasmic reticulum.

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

Access options

Rent or buy this article

Prices vary by article type

from$1.95

to$39.95

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

Similar content being viewed by others

References

  1. Hurtley, S. M. & Helenius, A. A. Rev. Cell Biol. 5, 277–307 (1989).

    Article  CAS  Google Scholar 

  2. Gething, M.-J. & Sambrook, J. Nature 355, 33–45 (1992).

    Article  ADS  CAS  Google Scholar 

  3. Helenius, A., Marquardt, T. & Braakman, I. Trends Cell Biol. 2, 227–231 (1992).

    Article  CAS  Google Scholar 

  4. Lodish, H. F., Kong, N., Snider, M. & Strous, G. J. A. M. Nature 304, 80–83 (1983).

    Article  ADS  CAS  Google Scholar 

  5. Lodish, H. F. J. biol. Chem. 263, 2107–2110 (1988).

    CAS  PubMed  Google Scholar 

  6. Pelham, H. R. B. A. Rev. Cell Biol. 5, 1–23 (1989).

    Article  CAS  Google Scholar 

  7. Wada, I. et al. J. biol. Chem. 226, 19599–19610 (1991).

    Google Scholar 

  8. Ahluwalia, N., Bergeron, J. J. M., Wada, I., Degen, E. & Williams, D. B. J. biol. Chem. 267, 10914–10918 (1992).

    CAS  PubMed  Google Scholar 

  9. Hochstenbach, F., David, V., Watkins, S. & Brenner, M. B. Proc. natn. Acad. Sci. U.S.A. 89, 4734–4738 (1992).

    Article  ADS  CAS  Google Scholar 

  10. Galvin, K. et al. Proc. natn. Acad. Sci. U.S.A. 89, 8452–8456 (1992).

    Article  ADS  CAS  Google Scholar 

  11. David, V., Hochstenbach, F., Rajagopalan, S. & Brenner, M. B. J. biol. Chem. 268, 9585–9592 (1993).

    CAS  PubMed  Google Scholar 

  12. Knowles, B. B., Howe, C. D. & Aden, D. P. Science 209, 497–499 (1980).

    Article  ADS  CAS  Google Scholar 

  13. Law, S. W. & Dugaiczyk, A. Nature 291, 201–205 (1981).

    Article  ADS  CAS  Google Scholar 

  14. Braakman, I., Hoover-Litty, H., Wagner, K. R. & Helenius, A. J. Cell Biol. 114, 401–411 (1991).

    Article  CAS  Google Scholar 

  15. Beckmann, R. P., Mizzen, L. A. & Welch, W. J. Science 248, 850–854 (1990).

    Article  ADS  CAS  Google Scholar 

  16. Lodish, H. F. & Kong, N. J. biol. Chem. 266, 14835–14838 (1991).

    CAS  PubMed  Google Scholar 

  17. Redman, C. M. & Cherian, M. G. J. Cell Biol. 52, 231–245 (1972).

    Article  CAS  Google Scholar 

  18. Machamer, C. E. & Rose, J. K. J. biol. Chem. 263, 5955–5960 (1988).

    CAS  PubMed  Google Scholar 

  19. Matzuk, M. M. & Boïme, I. J. Cell Biol. 106, 1049–1059 (1988).

    Article  CAS  Google Scholar 

  20. Weitz, G. & Proia, R. L. J. biol. Chem. 267, 10039–10044 (1992).

    CAS  PubMed  Google Scholar 

  21. Gething, M.-J., McCammon, K. & Sambrook, J. Cell 46, 939–950 (1986).

    Article  CAS  Google Scholar 

  22. Dorner, A. J., Bole, D. G. & Kaufman, R. J. J. Cell Biol. 105, 2665–2674 (1987).

    Article  CAS  Google Scholar 

  23. Hurtley, S. M., Bole, D. G., Hoover-Litty, H., Helenius, A. & Copeland, C. S. J. Cell Biol. 108, 2117–2126 (1989).

    Article  CAS  Google Scholar 

  24. Machamer, C. E., Doms, R. W., Bole, D. G., Helenius, A. & Rose, J. K. J. biol. Chem. 265, 6879–6883 (1990).

    CAS  PubMed  Google Scholar 

  25. Kim, P. S., Bole, D. & Arvan, P. J. Cell Biol. 118, 541–549 (1992).

    Article  CAS  Google Scholar 

  26. Marquardt, T. & Helenius, A. J. Cell Biol. 117, 505–513 (1992).

    Article  CAS  Google Scholar 

  27. Braakman, I., Helenius, J. & Helenius, A. Nature 356, 260–262 (1992).

    Article  ADS  CAS  Google Scholar 

  28. Degen, E. & Williams, D. B. J. Cell biol. 112, 1099–1115 (1991).

    Article  CAS  Google Scholar 

  29. Lodish, H. F. & Kong, N. J. Cell Biol. 98, 1720–1729 (1984).

    Article  CAS  Google Scholar 

  30. Brown, C. R., Martin, R. L., Hansen, W. J., Beckmann, R. P. & Welch, W. J. J. Cell Biol. 120, 1101–1112 (1993).

    Article  CAS  Google Scholar 

  31. Manning-Kreig, U. C., Scherer, P. E. & Schatz, G. EMB0 J. 10, 3273–3280 (1991).

    Article  Google Scholar 

  32. Langer, T. et al. Nature 356, 683–689 (1992).

    Article  ADS  CAS  Google Scholar 

  33. Amara, J. F., Cheng, S. H. & Smith, A, E. Trends Cell Biol. 2, 145–149 (1992).

    Article  CAS  Google Scholar 

  34. Callea, F., Brisigotti, M., Fabbretti, G., Bonino, F. & Desmet, V. J. Liver 12, 357–362 (1992).

    Article  CAS  Google Scholar 

  35. Degen, E., Cohen-Doyle, M. F. & Williams, D. B. J. exp. Med. 175, 1653–1661 (1992).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ou, WJ., Cameron, P., Thomas, D. et al. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364, 771–776 (1993). https://doi.org/10.1038/364771a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/364771a0

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

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