安普克
磷酸化
脂质代谢
蛋白激酶A
AMP活化蛋白激酶
脂解
细胞生物学
异三聚体G蛋白
蛋白质磷酸化
激酶
分解代谢
化学
合成代谢
信号转导
生物化学
生物
新陈代谢
G蛋白
脂肪组织
作者
Qi Wang,Shudong Liu,Aihua Zhai,Bai Zhang,Guizhen Tian
标识
DOI:10.1248/bpb.b17-00724
摘要
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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