IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v9y2018i1d10.1038_s41467-018-06003-9.html
   My bibliography  Save this article

AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum

Author

Listed:
  • Marie-Christine Klein

    (Saarland University)

  • Katharina Zimmermann

    (CIPMM Saarland University)

  • Stefan Schorr

    (Saarland University)

  • Martina Landini

    (Technical University Kaiserslautern)

  • Patrick A. W. Klemens

    (Technical University Kaiserslautern)

  • Jacqueline Altensell

    (Technical University Kaiserslautern)

  • Martin Jung

    (Saarland University)

  • Elmar Krause

    (CIPMM Saarland University)

  • Duy Nguyen

    (Saarland University)

  • Volkhard Helms

    (Saarland University)

  • Jens Rettig

    (CIPMM Saarland University)

  • Claudia Fecher-Trost

    (Saarland University)

  • Adolfo Cavalié

    (Saarland University)

  • Markus Hoth

    (CIPMM Saarland University)

  • Ivan Bogeski

    (CIPMM Saarland University
    University Medical Center, University of Göttingen)

  • H. Ekkehard Neuhaus

    (Technical University Kaiserslautern)

  • Richard Zimmermann

    (Saarland University)

  • Sven Lang

    (Saarland University)

  • Ilka Haferkamp

    (Technical University Kaiserslautern)

Abstract

To fulfill its role in protein biogenesis, the endoplasmic reticulum (ER) depends on the Hsp70-type molecular chaperone BiP, which requires a constant ATP supply. However, the carrier that catalyzes ATP uptake into the ER was unknown. Here, we report that our screen of gene expression datasets for member(s) of the family of solute carriers that are co-expressed with BiP and are ER membrane proteins identifies SLC35B1 as a potential candidate. Heterologous expression of SLC35B1 in E. coli reveals that SLC35B1 is highly specific for ATP and ADP and acts in antiport mode. Moreover, depletion of SLC35B1 from HeLa cells reduces ER ATP levels and, as a consequence, BiP activity. Thus, human SLC35B1 may provide ATP to the ER and was named AXER (ATP/ADP exchanger in the ER membrane). Furthermore, we propose an ER to cytosol low energy response regulatory axis (termed lowER) that appears as central for maintaining ER ATP supply.

Suggested Citation

  • Marie-Christine Klein & Katharina Zimmermann & Stefan Schorr & Martina Landini & Patrick A. W. Klemens & Jacqueline Altensell & Martin Jung & Elmar Krause & Duy Nguyen & Volkhard Helms & Jens Rettig &, 2018. "AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06003-9
    DOI: 10.1038/s41467-018-06003-9
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-018-06003-9
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-018-06003-9?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:9:y:2018:i:1:d:10.1038_s41467-018-06003-9. 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.