IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v8y2017i1d10.1038_s41467-017-00082-w.html
   My bibliography  Save this article

ATP-dependent modulation of MgtE in Mg2+ homeostasis

Author

Listed:
  • Atsuhiro Tomita

    (The University of Tokyo)

  • Mingfeng Zhang

    (Fudan University)

  • Fei Jin

    (Fudan University)

  • Wenhui Zhuang

    (Fudan University)

  • Hironori Takeda

    (Kyoto Sangyo University, Kamigamo-motoyama)

  • Tatsuro Maruyama

    (The University of Tokyo, Hongo)

  • Masanori Osawa

    (The University of Tokyo, Hongo)

  • Ken-ichi Hashimoto

    (Tokyo Denki University)

  • Hisashi Kawasaki

    (Tokyo Denki University)

  • Koichi Ito

    (The University of Tokyo)

  • Naoshi Dohmae

    (RIKEN Center for Sustainable Resource Science)

  • Ryuichiro Ishitani

    (The University of Tokyo)

  • Ichio Shimada

    (The University of Tokyo, Hongo)

  • Zhiqiang Yan

    (Fudan University
    Southwest Medical University)

  • Motoyuki Hattori

    (Fudan University)

  • Osamu Nureki

    (The University of Tokyo)

Abstract

Magnesium is an essential ion for numerous physiological processes. MgtE is a Mg2+ selective channel involved in the maintenance of intracellular Mg2+ homeostasis, whose gating is regulated by intracellular Mg2+ levels. Here, we report that ATP binds to MgtE, regulating its Mg2+-dependent gating. Crystal structures of MgtE–ATP complex show that ATP binds to the intracellular CBS domain of MgtE. Functional studies support that ATP binding to MgtE enhances the intracellular domain affinity for Mg2+ within physiological concentrations of this divalent cation, enabling MgtE to function as an in vivo Mg2+ sensor. ATP dissociation from MgtE upregulates Mg2+ influx at both high and low intracellular Mg2+ concentrations. Using site-directed mutagenesis and structure based-electrophysiological and biochemical analyses, we identify key residues and main structural changes involved in the process. This work provides the molecular basis of ATP-dependent modulation of MgtE in Mg2+ homeostasis.

Suggested Citation

  • Atsuhiro Tomita & Mingfeng Zhang & Fei Jin & Wenhui Zhuang & Hironori Takeda & Tatsuro Maruyama & Masanori Osawa & Ken-ichi Hashimoto & Hisashi Kawasaki & Koichi Ito & Naoshi Dohmae & Ryuichiro Ishita, 2017. "ATP-dependent modulation of MgtE in Mg2+ homeostasis," Nature Communications, Nature, vol. 8(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00082-w
    DOI: 10.1038/s41467-017-00082-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-017-00082-w
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-017-00082-w?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. Louis Tung Faat Lai & Jayashree Balaraman & Fei Zhou & Doreen Matthies, 2023. "Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms," Nature Communications, Nature, vol. 14(1), pages 1-10, 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:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00082-w. 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.