Anabolism

Phosphorylation

Heterotrimeric G protein

Lipolysis

Adipose tissue

Kinase

Chemistry

AMP-activated protein kinase

AMPK

Lipid metabolism

Biochemistry

Metabolism

Signal transduction

G protein

Biology

Protein phosphorylation

Cell biology

Catabolism

Protein kinase A

Biological and Pharmaceutical Bulletin

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.

AMPK-Mediated Regulation of Lipid Metabolism by Phosphorylation