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Interaction of AMP-activated protein kinase subunits in the heterotrimeric complex and with their yeast homologues.

AMP-activated protein kinase (AMPK) plays a key role in the regulation of fatty acid and cholesterol biosynthesis. It exists as a heterotrimeric complex, a catalytic subunit (AMPKa) and the two regulatory subunits (AMPKP and AMPKy) [1,2]. The activity of AMPK is stimulated allosterically (>5 fold) by micromolar concentrations of AMP and (>20 fold) when phosphorylated by an upstream kinase (AMPK kinase) [3]. The fact that AMPK is stimulated by AMP has led to the hypothesis that it functions as a cellular fuel gauge, shutting down the lipid biosynthetic pathway which deplete ATP, thus conserving ATP for essential cellular functions such as the maintenance of an ionic gradient [4].