Wang Qi, Liu Shudong, Zhai Aihua, Zhang Bai, Tian Guizhen
Department of Pharmacy, The Fifth People's Hospital of Jinan.
Department of Endocrinology, Shandong Rongjun General Hospital.
Biol Pharm Bull. 2018 Jul 1;41(7):985-993. doi: 10.1248/bpb.b17-00724. Epub 2018 Apr 28.
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.
AMP激活的蛋白激酶（AMPK）是哺乳动物中的一种代谢传感器，当细胞内ATP水平降低时被激活。AMPK是一种异源三聚体蛋白，由3个亚基组成，每个亚基都有多个磷酸化位点，这些位点通过直接磷酸化蛋白质或在多个途径（如脂质的合成、氧化和脂解）中调节基因转录，在合成代谢或分解代谢的调节中发挥关键作用。专注于参与脂质代谢的磷酸化位点的研究将有助于更好地认识AMPK在几种常见疾病治疗中的作用。在这篇综述中，我们密切关注了关于AMPK亚基的结构、多位点磷酸化以及AMPK通过相关分子的磷酸化对脂质代谢的调节的最新研究。
