Structure of mammalian AMPK and its regulation by ADP
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. Howell,
Rein Aasland,
Stephen R. Martin,
David Carling () and
Steven J. Gamblin ()
Additional contact information
Bing Xiao: MRC National Institute for Medical Research, The Ridgeway, Mill Hill
Matthew J. Sanders: MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College
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
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
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
Nature, 2011, vol. 472, issue 7342, 230-233
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.
Date: 2011
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:472:y:2011:i:7342:d:10.1038_nature09932
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DOI: 10.1038/nature09932
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