Publication Date:
2011-06-18
Description:
The adenosine monophosphate (AMP)-activated protein kinase (AMPK) regulates whole-body and cellular energy balance in response to energy demand and supply. AMPK is an alphabetagamma heterotrimer activated by decreasing concentrations of adenosine triphosphate (ATP) and increasing AMP concentrations. AMPK activation depends on phosphorylation of the alpha catalytic subunit on threonine-172 (Thr(172)) by kinases LKB1 or CaMKKbeta, and this is promoted by AMP binding to the gamma subunit. AMP sustains activity by inhibiting dephosphorylation of alpha-Thr(172), whereas ATP promotes dephosphorylation. Adenosine diphosphate (ADP), like AMP, bound to gamma sites 1 and 3 and stimulated alpha-Thr(172) phosphorylation. However, in contrast to AMP, ADP did not directly activate phosphorylated AMPK. In this way, both ADP/ATP and AMP/ATP ratios contribute to AMPK regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oakhill, Jonathan S -- Steel, Rohan -- Chen, Zhi-Ping -- Scott, John W -- Ling, Naomi -- Tam, Shanna -- Kemp, Bruce E -- New York, N.Y. -- Science. 2011 Jun 17;332(6036):1433-5. doi: 10.1126/science.1200094.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Chemistry and Metabolism, St. Vincent's Institute of Medical Research, University of Melbourne, 41 Victoria Parade, Fitzroy 3065, Victoria, Australia. joakhill@svi.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21680840" target="_blank"〉PubMed〈/a〉
Keywords:
AMP-Activated Protein Kinases/chemistry/*metabolism
;
Adenosine Diphosphate/*metabolism
;
Adenosine Monophosphate/*metabolism
;
Adenosine Triphosphate/*metabolism
;
Animals
;
Binding Sites
;
COS Cells
;
Calcium-Calmodulin-Dependent Protein Kinase Kinase/metabolism
;
Cercopithecus aethiops
;
Enzyme Activation
;
Myristic Acid/metabolism
;
Phosphorylation
;
Protein Subunits/chemistry/metabolism
;
Protein-Serine-Threonine Kinases/metabolism
;
Recombinant Fusion Proteins/metabolism
;
Threonine/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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