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:

A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum

Nature volume 365, pages 176–179 (1993)Cite this article

Abstract

UBIQUITIN-conjugating enzymes function in selective proteolysis pathways and catalyse the covalent attachment of ubiquitin to proteolytic substrates1–4. Here we report the identification of an integral membrane ubiquitin-conjugating enzyme. This enzyme, UBC6, localizes to the endoplasmic reticulum (ER), with the cata-lytic domain facing the cytosol. ubc6 loss-of-function mutants sup-press the protein translocation defect caused by a mutation in SEC61, which encodes a key component of a multisubunit protein translocation apparatus of the ER5–11. The expression of the sec61 mutant phenotype requires both the activity of UBC6 and its localization at the ER membrane. This suggests that UBC6 may mediate selective degradation of ER membrane proteins and that the protein translocation defect of sec61 may be caused by proteolysis of components of a structurally distorted mutant translocation apparatus.

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. Finley, D. & Chau, V. A. Rev. Cell Biol. 7, 25–69 (1986).

    Article  Google Scholar 

  2. Hershko, A. Trends biochem. Sci. 16, 265–268 (1991).

    Article  CAS  Google Scholar 

  3. Jentsch, S. Trends Cell Blol. 2, 98–103 (1992).

    Article  CAS  Google Scholar 

  4. Jentsch, S. A. Rev. Genet. 26, 177–205 (1992).

    Article  Google Scholar 

  5. Deshaies, R. J. & Schekman, R. J. Cell Biol. 105, 633–645 (1987).

    Article  CAS  Google Scholar 

  6. Deshaies, R. J., Sanders, S. L., Feldheim, D. A. & Schekman, R. Nature 349, 806–808 (1991).

    Article  ADS  CAS  Google Scholar 

  7. Stirling, C. J., Rothblatt, J., Hosobuchi, M., Deshaies, R. & Schekman, R. Molec. Biol. Cell 3, 129–142 (1992).

    Article  CAS  Google Scholar 

  8. Sanders, S. L., Whitfield, K. M., Vogel, J. P., Rose, M. D. & Schekman, R. W. Cell 69, 353–365 (1992).

    Article  CAS  Google Scholar 

  9. Müsch, A., Wiedmann, M. & Rapoport, T. A. Cell 69, 343–352 (1992).

    Article  Google Scholar 

  10. Görlich, D., Prehn, S., Hartmann, E., Kalles, K.-U. & Rapoport, T. A. Cell 71, 489–503 (1992).

    Article  Google Scholar 

  11. Rothblatt, J. A., Deshaies, R. J., Sanders, S. L., Daum, G. & Schekman, R. J. Cell Biol. 109, 2641–2652 (1989).

    Article  CAS  Google Scholar 

  12. Kutay, U., Hartmann, E. & Rapoport, T. Trends Cell Biol. 3, 72–75 (1993).

    Article  CAS  Google Scholar 

  13. Jentsch, S., McGrath, J. P. & Varshavsky, A. Nature 329, 131–134 (1987).

    Article  ADS  CAS  Google Scholar 

  14. Goebl, M. G. et al. Science 241, 1331–1335 (1988).

    Article  ADS  CAS  Google Scholar 

  15. Seufert, W. & Jentsch, S. EMBO J. 9, 543–550 (1990).

    Article  CAS  Google Scholar 

  16. Seufert, W., McGrath, J. P. & Jentsch, S. EMBO J. 9, 4535–4541 (1990).

    Article  CAS  Google Scholar 

  17. Wiebel, F. F. & Kunau, W.-H. Nature 359, 73–76 (1992).

    Article  ADS  CAS  Google Scholar 

  18. Jungmann, J., Reins, H.-A., Schobert, C. & Jentsch, S. Nature 361, 369–371 (1993).

    Article  ADS  CAS  Google Scholar 

  19. Rose, M. C., Misra, L. M. & Vogel, J. P. Cell 57, 1211–1221 (1989).

    Article  CAS  Google Scholar 

  20. Dohmen, R. J., Madura, K., Bartel, B. & Varshavsky, A. Proc. natn. Acad. Sci. U.S.A. 88, 7351–7355 (1991).

    Article  ADS  CAS  Google Scholar 

  21. Chen, P., Johnson, P., Sommer, T., Jentsch, S., Hochstrasser, M. Cell 74, 357–369 (1993).

    Article  CAS  Google Scholar 

  22. Klausner, R. D. & Sitia, R. Cell 62, 611–614 (1990).

    Article  CAS  Google Scholar 

  23. Bonifacino, J. S. & Lippincott-Schwartz, J. Curr. Biol. 3, 592–600 (1991).

    Article  CAS  Google Scholar 

  24. Cheng, S. H. et al. Cell 63, 827–834 (1990).

    Article  CAS  Google Scholar 

  25. Goldberg, A. L. & Rock, K. L. Nature 357, 375–379 (1992).

    Article  ADS  CAS  Google Scholar 

  26. Tierney, D. J., Haas, A. L. & Koop, D. R. Arch. Biochem. Biophys. 293, 9–16 (1992).

    Article  CAS  Google Scholar 

  27. Roberts, C. J., Nothwehr, S. F. & Stevens, T. J. Cell Biol. 119, 69–83 (1992).

    Article  CAS  Google Scholar 

  28. Ausubel, F. M. et al. (eds) Current Protocols in Molecular Biology (Green and Wiley, New York, 1992).

  29. Field, J. et al. Molec. cell. Biol. 8, 2159–2165 (1988).

    Article  CAS  Google Scholar 

  30. Guthrie, C. & Fink G. R. (eds) Guide to Yeast Genetics and Molecular Biology (Academic, San Diego, 1991).

Download references

Author information

Author notes

  1. Thomas Sommer

    Present address: Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, 13125, Berlin-Buch, Germany

  2. Stefan Jentsch

    Present address: ZMBH, University of Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany

Authors and Affiliations

  1. Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft, Spemannstrasse, 37-39, 72076, Tübingen, Germany

    Thomas Sommer & Stefan Jentsch

Authors
  1. Thomas Sommer
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Stefan Jentsch
    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

Sommer, T., Jentsch, S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365, 176–179 (1993). https://doi.org/10.1038/365176a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/365176a0

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