IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v465y2010i7296d10.1038_nature09003.html
   My bibliography  Save this article

eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation

Author

Listed:
  • Martin D. Jennings

    (Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK)

  • Graham D. Pavitt

    (Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK)

Abstract

Translation initiation by eIF2 The translation factor that helps deliver the initiator tRNA to the ribosome, eIF2, uses the energy of GTP hydrolysis for function. Another factor, eIF5, was known to accelerate the GTPase activity of eIF2 when it was bound to the initiator tRNA and the ribosome. In this study two other roles for eIF5 have been defined. One involves stabilizing the binding of GDP, the product of GTP hydrolysis, to eIF2. The other involves its acting with phosphorylated eIF2 to inhibit the guanine nucleotide exchange factor, eIF2B. These results clarify our understanding of how translation initiation is regulated.

Suggested Citation

  • Martin D. Jennings & Graham D. Pavitt, 2010. "eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation," Nature, Nature, vol. 465(7296), pages 378-381, May.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7296:d:10.1038_nature09003
    DOI: 10.1038/nature09003
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09003
    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/nature09003?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. Hui-Hsien Chang & Lin-Chen Huang & Karen S. Browning & Enamul Huq & Mei-Chun Cheng, 2024. "The phosphorylation of carboxyl-terminal eIF2α by SPA kinases contributes to enhanced translation efficiency during photomorphogenesis," Nature Communications, Nature, vol. 15(1), pages 1-18, 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:465:y:2010:i:7296:d:10.1038_nature09003. 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.