Biolegend, 600656, Alexa Fluor® 647 anti-AMPKα Phospho (Thr172)

AMP-activated protein kinase alpha (AMPKα) is one subunit of the αβγ heterotrimeric protein complex AMPK. It is a key regulator of metabolism and energy homeostasis in eukaryotes through induction of catabolic pathways and deactivation of anabolic. As an inhibitor of mammalian target of rapamycin complex 1 (mTORC1) pathway, AMPKα is involved in the regulation of cellular growth, cell cycle progression, autophagy, and may play dual roles as both tumor suppressor and promotor. AMPKα is activated via phosphorylation of Threonine residue 172 (Thr172) within the activation loop of the α subunit and is promoted by the allosteric binding of AMP and/or ADP to AMPK’s γ subunit. This phosphorylation is mediated by the serine/threonine kinase liver kinase B1 (LKB1) in conjunction with accessory subunits STRAD and MO25 and also by calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2 aka CAMKKβ). Activation is induced by increases in cellular AMP:ATP and ADP:ATP ratios  following a decline in ATP levels as well as by cellular stress, DNA damage, glucose starvation, and fluxes in calcium and nutrient levels. Localization of AMPKα Thr172 at the spindle poles suggests a novel role for AMPK in mitotic spindle orientation. AMPKα is a key therapeutic target in the treatment of metabolic disorders and an emerging potential treatment target for cancer.