IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms11952.html
   My bibliography  Save this article

Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A

Author

Listed:
  • Metin Aksu

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Sergei Trakhanov

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Dirk Görlich

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

Abstract

Xpo4 is a bidirectional nuclear transport receptor that mediates nuclear export of eIF5A and Smad3 as well as import of Sox2 and SRY. How Xpo4 recognizes such a variety of cargoes is as yet unknown. Here we present the crystal structure of the RanGTP·Xpo4·eIF5A export complex at 3.2 Å resolution. Xpo4 has a similar structure as CRM1, but the NES-binding site is occluded, and a new interaction site evolved that recognizes both globular domains of eIF5A. eIF5A contains hypusine, a unique amino acid with two positive charges, which is essential for cell viability and eIF5A function in translation. The hypusine docks into a deep, acidic pocket of Xpo4 and is thus a critical element of eIF5A’s complex export signature. This further suggests that Xpo4 recognizes other cargoes differently, and illustrates how Xpo4 suppresses – in a chaperone-like manner – undesired interactions of eIF5A inside nuclei.

Suggested Citation

  • Metin Aksu & Sergei Trakhanov & Dirk Görlich, 2016. "Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A," Nature Communications, Nature, vol. 7(1), pages 1-10, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11952
    DOI: 10.1038/ncomms11952
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms11952
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms11952?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
    ---><---

    Citations

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


    Cited by:

    1. Elżbieta Wątor & Piotr Wilk & Artur Biela & Michał Rawski & Krzysztof M. Zak & Wieland Steinchen & Gert Bange & Sebastian Glatt & Przemysław Grudnik, 2023. "Cryo-EM structure of human eIF5A-DHS complex reveals the molecular basis of hypusination-associated neurodegenerative disorders," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Moreira, Carlos Alves & Philot, Eric Allison & Lima, Angélica Nakagawa & Scott, Ana Ligia, 2019. "Predicting regions prone to protein aggregation based on SVM algorithm," Applied Mathematics and Computation, Elsevier, vol. 359(C), pages 502-511.

    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:7:y:2016:i:1:d:10.1038_ncomms11952. 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.