AMPK is a direct adenylate charge-regulated protein kinase.

Article Details


Oakhill JS, Steel R, Chen ZP, Scott JW, Ling N, Tam S, Kemp BE

AMPK is a direct adenylate charge-regulated protein kinase.

Science. 2011 Jun 17;332(6036):1433-5. doi: 10.1126/science.1200094.

PubMed ID
21680840 [ View in PubMed

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.

DrugBank Data that Cites this Article

NameUniProt ID
5'-AMP-activated protein kinase subunit beta-1Q9Y478Details
5'-AMP-activated protein kinase catalytic subunit alpha-1Q13131Details
5'-AMP-activated protein kinase subunit gamma-1P54619Details