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Adenylate-activated protein kinase (AMPK) is a key molecule in the regulation of bioenergy metabolism which exists as a heterotrimeric complex consist of an α-catalytic subunit, a β-regulatory subunit, and a γ-regulatory the composition of subunits. The N-terminus of the α-subunit contains a conserved Ser/Thr kinase domain, and a conserved threonine (Thr-172) site, the phosphorylation of which is required for its kinase activity. The major upstream phosphorylases are AMP-dependent STK11 and Ca2+-dependent CAMKK. AMPK is expressed in a variety of metabolically related organs and can be activated by various body stimuli, including cellular stress, exercise, hormones and substances that can affect cell metabolism. Genetic and pharmacological studies have shown that AMPK is essential for the body to keep glucose balance and is central to the study of diabetes and other metabolic-related diseases.
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