IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms12897.html
   My bibliography  Save this article

PRMT1-mediated methylation of MICU1 determines the UCP2/3 dependency of mitochondrial Ca2+ uptake in immortalized cells

Author

Listed:
  • Corina T. Madreiter-Sokolowski

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Christiane Klec

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Warisara Parichatikanond

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz
    Present address: Department of Pharmacology, Mahidol University, Bangkok 10400, Thailand)

  • Sarah Stryeck

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Benjamin Gottschalk

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Sergio Pulido

    (Institute of Chemistry, University of Graz)

  • Rene Rost

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Emrah Eroglu

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Nicole A. Hofmann

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Alexander I. Bondarenko

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Tobias Madl

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz
    Center for Integrated Protein Science, Technical University Munich
    Institute of Structural Biology, Helmholtz Zentrum München)

  • Markus Waldeck-Weiermair

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Roland Malli

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

  • Wolfgang F. Graier

    (Center for Molecular Medicine, Institute of Molecular Biology and Biochemistry, Medical University of Graz)

Abstract

Recent studies revealed that mitochondrial Ca2+ channels, which control energy flow, cell signalling and death, are macromolecular complexes that basically consist of the pore-forming mitochondrial Ca2+ uniporter (MCU) protein, the essential MCU regulator (EMRE), and the mitochondrial Ca2+ uptake 1 (MICU1). MICU1 is a regulatory subunit that shields mitochondria from Ca2+ overload. Before the identification of these core elements, the novel uncoupling proteins 2 and 3 (UCP2/3) have been shown to be fundamental for mitochondrial Ca2+ uptake. Here we clarify the molecular mechanism that determines the UCP2/3 dependency of mitochondrial Ca2+ uptake. Our data demonstrate that mitochondrial Ca2+ uptake is controlled by protein arginine methyl transferase 1 (PRMT1) that asymmetrically methylates MICU1, resulting in decreased Ca2+ sensitivity. UCP2/3 normalize Ca2+ sensitivity of methylated MICU1 and, thus, re-establish mitochondrial Ca2+ uptake activity. These data provide novel insights in the complex regulation of the mitochondrial Ca2+ uniporter by PRMT1 and UCP2/3.

Suggested Citation

  • Corina T. Madreiter-Sokolowski & Christiane Klec & Warisara Parichatikanond & Sarah Stryeck & Benjamin Gottschalk & Sergio Pulido & Rene Rost & Emrah Eroglu & Nicole A. Hofmann & Alexander I. Bondaren, 2016. "PRMT1-mediated methylation of MICU1 determines the UCP2/3 dependency of mitochondrial Ca2+ uptake in immortalized cells," Nature Communications, Nature, vol. 7(1), pages 1-13, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12897
    DOI: 10.1038/ncomms12897
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms12897
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms12897?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:7:y:2016:i:1:d:10.1038_ncomms12897. 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.