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The 5'-AMP-activated protein kinase (AMPK), a member of the SNF1 (sucrose non-fermentor) kinase family (1), is a heterotrimeric protein comprise of alpha (63 kDa), beta (30 kDa) and gamma (38 kDa) subunits. The alpah subunit is the catalytic subunit, while beta and gamma are non-catalytic subunits (although they have been found to interact with the active subunit in liver). AMPK regulates fatty acid and sterol synthesis by phosphorylation of acetyl-CoA as well as cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (2). AMPK is activated by AMP and can be also regulated by treatment with purified protein phosphatase in vitro (3).
