IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v458y2009i7237d10.1038_nature07962.html
   My bibliography  Save this article

The ubiquitylation machinery of the endoplasmic reticulum

Author

Listed:
  • Christian Hirsch

    (Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10)

  • Robert Gauss

    (Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10)

  • Sabine C. Horn

    (Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10)

  • Oliver Neuber

    (Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10
    Present address: Institute for Genetics, University of Cologne, Zülpicher Strasse 47, 50674 Cologne, Germany.)

  • Thomas Sommer

    (Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10)

Abstract

As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains newly synthesized polypeptides and supports their maturation. Only properly folded proteins are released to their designated destinations. Proteins that cannot mature are left to accumulate, impairing the function of the ER. To maintain homeostasis, the protein-quality-control system singles out aberrant polypeptides and delivers them to the cytosol, where they are destroyed by the proteasome. The importance of this pathway is evident from the growing list of pathologies associated with quality-control defects in the ER.

Suggested Citation

  • Christian Hirsch & Robert Gauss & Sabine C. Horn & Oliver Neuber & Thomas Sommer, 2009. "The ubiquitylation machinery of the endoplasmic reticulum," Nature, Nature, vol. 458(7237), pages 453-460, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7237:d:10.1038_nature07962
    DOI: 10.1038/nature07962
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07962
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature07962?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Shuai Chen & Cai-Xia Pei & Si Xu & Hanjie Li & Yi-Shi liu & Yicheng Wang & Cheng Jin & Neta Dean & Xiao-Dong Gao, 2024. "Rft1 catalyzes lipid-linked oligosaccharide translocation across the ER membrane," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:458:y:2009:i:7237:d:10.1038_nature07962. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.