AMP-activated protein kinase (AMPK; EC 2.7.11.31) is a heterotrimeric enzyme with a key role in regulating cellular energy metabolism, cell growth and cell polarity. In response to a change in the intracellular AMP:ATP or ADP:ATP ratios it activates energy-producing pathways and inhibits energy-consuming processes. Furthermore, AMPK is regulated by a diverse range of hormones among which leptin, adiponectin, ciliary neurotrophic factor and ghrelin. Of the three subunits α, β, and γ that constitute the protein kinase, the α-subunit hosts the catalytic domain, while the latter two subunits β, and γ fulfill a regulatory function. Activation of AMPK is triggered by phosphorylation of a threonine residue, which lies in the activation segment of the amino-terminal kinase domain of the α-subunit and results in a several-hundred-fold increase in activity. In mammals, calcium/calmodulin-dependent protein kinase kinase-β (CaMKKβ), LKB1, and transforming growth factor-β-activated kinase 1 (TAK1)  are the predominant kinases upstream of AMPK[1]. In turn, activated, phosphorylated AMPK can be inactivated by protein phosphatases (PP), e.g. PP2A, PP2Cα and Ppm1E. Currently, AMPK is viewed as an important molecular target since it is believed that novel AMPK modulators may be useful in the therapy of cancer, metabolic, and neurodegenerative diseases, such as type 2 diabetes, Alzheimer’s disease, and aging[2],[3].