AMPK is a direct adenylate charge-regulated protein kinase
Journal article
Oakhill, Jonathan S., Steel, Rohan, Chen, Zhi-Ping, Scott, John W., Ling, Naomi, Tam, Shanna and Kemp, Bruce Ernest. (2011). AMPK is a direct adenylate charge-regulated protein kinase. Science. 332(6036), pp. 1433 - 1435. https://doi.org/10.1126/science.1200094
Authors | Oakhill, Jonathan S., Steel, Rohan, Chen, Zhi-Ping, Scott, John W., Ling, Naomi, Tam, Shanna and Kemp, Bruce Ernest |
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Abstract | 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 αβγ heterotrimer activated by decreasing concentrations of adenosine triphosphate ( ATP ) and increasing AMP concentrations. AMPK activation depends on phosphorylation of the α catalytic subunit on threonine-172 ( Thr172 ) by kinases LKB1 or CaMKKβ, and this is promoted by AMP binding to the γ subunit. AMP sustains activity by inhibiting dephosphorylation of α-Thr172, whereas ATP promotes dephosphorylation. Adenosine diphosphate ( ADP ), like AMP, bound to γ sites 1 and 3 and stimulated α-Thr172 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. |
Year | 2011 |
Journal | Science |
Journal citation | 332 (6036), pp. 1433 - 1435 |
Publisher | American Association for the Advancement of Science |
ISSN | 0036-8075 |
Digital Object Identifier (DOI) | https://doi.org/10.1126/science.1200094 |
Scopus EID | 2-s2.0-79959338922 |
Page range | 1433 - 1435 |
Publisher's version | File Access Level Controlled |
Place of publication | United States of America |
https://acuresearchbank.acu.edu.au/item/8578w/ampk-is-a-direct-adenylate-charge-regulated-protein-kinase
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