Hardie D Grahame
Division of Molecular Physiology, Wellcome Trust Biocentre, University of Dundee, Dow Street, Dundee, DD1 4HN, Scotland, UK.
Curr Opin Cell Biol. 2005 Apr;17(2):167-73. doi: 10.1016/j.ceb.2005.01.006.
The AMP-activated protein kinase (AMPK) is a sensor of cellular energy that is conserved throughout eukaryotes. It is activated by rising AMP, signifying falling energy status caused by starvation for a carbon source or other stress. Binding of AMP to the regulatory gamma subunit triggers phosphorylation of the catalytic alpha subunit by the upstream kinase LKB1, and the activated kinase switches on ATP-generating catabolic pathways while switching off ATP-requiring processes. AMPK inhibits the TOR (target of rapamycin) pathway by phosphorylating TSC2, thus inhibiting cell growth during times of stress. AMPK is also a target for adipokines that regulate energy balance at the whole-body level.
AMP激活的蛋白激酶（AMPK）是一种细胞能量传感器，在整个真核生物中都保守存在。它通过AMP水平升高而被激活，这表明由于碳源饥饿或其他应激导致能量状态下降。AMP与调节性γ亚基结合会触发上游激酶LKB1对催化性α亚基的磷酸化，而激活的激酶会开启产生ATP的分解代谢途径，同时关闭需要ATP的过程。AMPK通过磷酸化TSC2来抑制雷帕霉素靶蛋白（TOR）途径，从而在应激期间抑制细胞生长。AMPK也是调节全身能量平衡的脂肪因子的作用靶点。
