IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v513y2014i7518d10.1038_nature13492.html
   My bibliography  Save this article

Coordinated regulation of protein synthesis and degradation by mTORC1

Author

Listed:
  • Yinan Zhang

    (Harvard School of Public Health)

  • Justin Nicholatos

    (Harvard School of Public Health)

  • John R. Dreier

    (Brigham and Women’s Hospital, Harvard Medical School)

  • Stéphane J. H. Ricoult

    (Harvard School of Public Health)

  • Scott B. Widenmaier

    (Harvard School of Public Health)

  • Gökhan S. Hotamisligil

    (Harvard School of Public Health)

  • David J. Kwiatkowski

    (Brigham and Women’s Hospital, Harvard Medical School)

  • Brendan D. Manning

    (Harvard School of Public Health)

Abstract

mTORC1 is known to stimulate protein synthesis; now, it is shown to also promote the synthesis of proteasomes, which degrade proteins into the amino acids needed to create new proteins.

Suggested Citation

  • Yinan Zhang & Justin Nicholatos & John R. Dreier & Stéphane J. H. Ricoult & Scott B. Widenmaier & Gökhan S. Hotamisligil & David J. Kwiatkowski & Brendan D. Manning, 2014. "Coordinated regulation of protein synthesis and degradation by mTORC1," Nature, Nature, vol. 513(7518), pages 440-443, September.
  • Handle: RePEc:nat:nature:v:513:y:2014:i:7518:d:10.1038_nature13492
    DOI: 10.1038/nature13492
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature13492
    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/nature13492?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. Maxime Uriarte & Nadine Nkwe & Roch Tremblay & Oumaima Ahmed & Clémence Messmer & Nazar Mashtalir & Haithem Barbour & Louis Masclef & Marion Voide & Claire Viallard & Salima Daou & Djaileb Abdelhadi &, 2021. "Starvation-induced proteasome assemblies in the nucleus link amino acid supply to apoptosis," Nature Communications, Nature, vol. 12(1), pages 1-22, 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:513:y:2014:i:7518:d:10.1038_nature13492. 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.