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. Author manuscript; available in PMC: 2012 Mar 2.
Published in final edited form as: Nat Cell Biol. 2011 Sep 2;13(9):1016–1023. doi: 10.1038/ncb2329

Figure 4. AMPK control of transcription.

Figure 4

AMPK regulates several physiological processes through phosphorylation of transcription factors and co-activators. It shares substrates with its AMPK family related kinases to negatively regulate gluconeogenesis in the liver by phosphorylation and inhibition of the CRCT2 and Class IIa HDACs. These phosphorylation events induce binding to 14-3-3 scaffold proteins and sequestration of these transcription regulators into the cytoplasm. AMPK also regulates transcription factors via inducing their degradation (Cry1), preventing their proteolytic activation and translocation to nucleus (Srebp1), and by disrupting protein-protein (p300) or protein-DNA interactions (Arebp, HNF4a). AMPK has also been shown to directly control phosphorylation of Histone 2B on Serine 36 as well as indirectly controlling SIRT1 activity via increasing NAD+ levels.