IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v4y2013i1d10.1038_ncomms3234.html

Some searches may not work properly. We apologize for the inconvenience.

   My bibliography  Save this article

Involvement of Bag6 and the TRC pathway in proteasome assembly

Author

Listed:
  • Takashi Akahane

    (Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo)

  • Kazutaka Sahara

    (Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo)

  • Hideki Yashiroda

    (Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo)

  • Keiji Tanaka

    (Laboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science)

  • Shigeo Murata

    (Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo)

Abstract

The 26S proteasome has an elaborate structure, consisting of 33 different subunits that form the 20S core particle capped by the 19S regulatory particle on either end. Several chaperones that are dedicated to the accurate assembly of this protease complex have been identified, but the mechanisms underlying proteasome biogenesis remain unexplored so far. Here we report that core particle assembly becomes less efficient if the TRC pathway, which mediates insertion of tail-anchored proteins, is defective. We demonstrate that Bag6, a protein in the TRC pathway that is also responsible for the degradation of mislocalized proteins, is not only involved in core particle assembly but also has a key role in efficient regulatory particle assembly by directly associating with precursor regulatory particles. These findings indicate that proteasome assembly is not solely mediated by dedicated chaperones but also depends on general chaperones that preserve protein homeostasis.

Suggested Citation

  • Takashi Akahane & Kazutaka Sahara & Hideki Yashiroda & Keiji Tanaka & Shigeo Murata, 2013. "Involvement of Bag6 and the TRC pathway in proteasome assembly," Nature Communications, Nature, vol. 4(1), pages 1-8, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3234
    DOI: 10.1038/ncomms3234
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms3234
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms3234?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
    ---><---

    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:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3234. 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.