Author
Listed:
- Bing Xiao
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- Matthew J. Sanders
(MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College
Present addresses: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK (M.J.S.); Department of Molecular Biology, University of Bergen, Thormöhlensgt. 55, N5020 Bergen, Norway (R.A.); Cancer Research UK, 44 Lincoln’s Inn Fields, PO Box 123, London WC2A 3PX, UK (P.S.).)
- Elizabeth Underwood
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- Richard Heath
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- Faith V. Mayer
(MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College)
- David Carmena
(MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College)
- Chun Jing
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- Philip A. Walker
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- John F. Eccleston
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- Lesley F. Haire
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- Peter Saiu
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill
Present addresses: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK (M.J.S.); Department of Molecular Biology, University of Bergen, Thormöhlensgt. 55, N5020 Bergen, Norway (R.A.); Cancer Research UK, 44 Lincoln’s Inn Fields, PO Box 123, London WC2A 3PX, UK (P.S.).)
- Steven A. Howell
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- Rein Aasland
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill
Present addresses: MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK (M.J.S.); Department of Molecular Biology, University of Bergen, Thormöhlensgt. 55, N5020 Bergen, Norway (R.A.); Cancer Research UK, 44 Lincoln’s Inn Fields, PO Box 123, London WC2A 3PX, UK (P.S.).)
- Stephen R. Martin
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
- David Carling
(MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College)
- Steven J. Gamblin
(MRC National Institute for Medical Research, The Ridgeway, Mill Hill)
Abstract
AMPK in energy metabolism AMP-activated protein kinase (AMPK) has an important role in regulating cellular energy metabolism; in response to a fall in intracellular ATP levels, it activates energy-producing pathways and inhibits energy-consuming processes. Here, a role for ADP in regulating AMPK by protecting the enzyme from dephosphorylation is defined, and a crystal structure of the active enzyme containing the kinase domain is presented. A model is proposed for how AMP and ADP regulate AMPK activity.
Suggested Citation
Bing Xiao & Matthew J. Sanders & Elizabeth Underwood & Richard Heath & Faith V. Mayer & David Carmena & Chun Jing & Philip A. Walker & John F. Eccleston & Lesley F. Haire & Peter Saiu & Steven A. Howe, 2011.
"Structure of mammalian AMPK and its regulation by ADP,"
Nature, Nature, vol. 472(7342), pages 230-233, April.
Handle:
RePEc:nat:nature:v:472:y:2011:i:7342:d:10.1038_nature09932
DOI: 10.1038/nature09932
Download full text from publisher
As the access to this document is restricted, you may want to search for a different version of it.
Citations
Citations are extracted by the
CitEc Project, subscribe to its
RSS feed for this item.
Cited by:
- Danielle L. Schmitt & Stephanie D. Curtis & Anne C. Lyons & Jin-fan Zhang & Mingyuan Chen & Catherine Y. He & Sohum Mehta & Reuben J. Shaw & Jin Zhang, 2022.
"Spatial regulation of AMPK signaling revealed by a sensitive kinase activity reporter,"
Nature Communications, Nature, vol. 13(1), pages 1-12, December.
- Eva Crosas-Molist & Vittoria Graziani & Oscar Maiques & Pahini Pandya & Joanne Monger & Remi Samain & Samantha L. George & Saba Malik & Jerrine Salise & Valle Morales & Adrien Le Guennec & R. Andrew A, 2023.
"AMPK is a mechano-metabolic sensor linking cell adhesion and mitochondrial dynamics to Myosin-dependent cell migration,"
Nature Communications, Nature, vol. 14(1), pages 1-22, December.
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:472:y:2011:i:7342:d:10.1038_nature09932. 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.