IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v459y2009i7250d10.1038_nature08075.html
   My bibliography  Save this article

Structural insight into the autoinhibition mechanism of AMP-activated protein kinase

Author

Listed:
  • Lei Chen

    (MOE Key Laboratory of Bioinformatics, Tsinghua University)

  • Zhi-Hao Jiao

    (MOE Key Laboratory of Bioinformatics, Tsinghua University)

  • Li-Sha Zheng

    (Institute of Biophysics and Graduate University, Chinese Academy of Sciences)

  • Yuan-Yuan Zhang

    (MOE Key Laboratory of Bioinformatics, Tsinghua University)

  • Shu-Tao Xie

    (MOE Key Laboratory of Bioinformatics, Tsinghua University)

  • Zhi-Xin Wang

    (MOE Key Laboratory of Bioinformatics, Tsinghua University
    Institute of Biophysics and Graduate University, Chinese Academy of Sciences)

  • Jia-Wei Wu

    (MOE Key Laboratory of Bioinformatics, Tsinghua University)

Abstract

Molecular mechanism AMPK autoinhibition mechanism AMPK (AMP-activated protein kinase) senses cellular energy status to maintain a balance between ATP production and consumption and has important roles in regulating cell growth and proliferation. Here, crystal structures of kinase and autoinhibitory domains from yeast AMPK subunits, together with biochemical data, reveal a mechanism for AMPK autoinhibition and suggest a model for allosteric activation by AMP.

Suggested Citation

  • Lei Chen & Zhi-Hao Jiao & Li-Sha Zheng & Yuan-Yuan Zhang & Shu-Tao Xie & Zhi-Xin Wang & Jia-Wei Wu, 2009. "Structural insight into the autoinhibition mechanism of AMP-activated protein kinase," Nature, Nature, vol. 459(7250), pages 1146-1149, June.
  • Handle: RePEc:nat:nature:v:459:y:2009:i:7250:d:10.1038_nature08075
    DOI: 10.1038/nature08075
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature08075
    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/nature08075?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.

    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:459:y:2009:i:7250:d:10.1038_nature08075. 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.