4.3 Review

AMPK-Mediated Regulation of Lipid Metabolism by Phosphorylation

Journal

BIOLOGICAL & PHARMACEUTICAL BULLETIN
Volume 41, Issue 7, Pages 985-993

Publisher

PHARMACEUTICAL SOC JAPAN
DOI: 10.1248/bpb.b17-00724

Keywords

AMP-activated protein kinase (AMPK); lipid metabolism; phosphorylation; fatty acid; review

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AMP-activated protein kinase (AMPK) is a metabolic sensor in mammals that is activated when ATP levels in the cell decrease. AMPK is a heterotrimeric protein that comprises 3 subunits, each of which has multiple phosphorylation sites that play critical roles in the regulation of either anabolism or catabolism by directly phosphorylating proteins or modulating gene transcription in multiple pathways, such as synthesis, oxidation and lipolysis of lipid. Research focused on the phosphorylation sites that are involved in lipid metabolism will lead to a better recognition of the role of AMPK in therapeutics for several common diseases. In this review, close attention is paid to the recent research on the structure, and multisite phosphorylation of AMPK subunits, as well as AMPK regulation of lipid metabolism via phosphorylation of related molecules.

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