Protein Chemistry and Metabolism, St Vincent's Institute and Department of Medicine, University of Melbourne, 41 Victoria Parade, Fitzroy, Victoria 3065, Australia.
Trends Endocrinol Metab. 2012 Mar;23(3):125-32. doi: 10.1016/j.tem.2011.12.006. Epub 2012 Jan 26.
The energy sensor AMP-activated protein kinase (AMPK) is activated by metabolic stress and restores ATP levels in cells by switching off anabolic and switching on catabolic pathways. Recent discoveries demonstrate that AMPK is activated primarily by rising ADP levels and not, as previously thought, by AMP. AMPK activation is dependent on ADP-controlled phosphorylation of Thr172 on its activation loop, a mechanism of protein regulation that represents an example of an allosterically regulated modification (ARM). AMPK embodies many features of an adenylate charge regulatory system envisaged by Atkinson, where anabolic and catabolic pathway regulation is modulated by adenine nucleotide ratios. Here we discuss the current state of AMPK regulation by adenine nucleotides and we propose that AMPK functions as an adenylate charge-regulated protein kinase.
能量传感器 AMP 激活蛋白激酶（AMPK）通过代谢应激激活，并通过关闭合成代谢途径和开启分解代谢途径来恢复细胞中的 ATP 水平。最近的发现表明，AMPK 的激活主要是由 ADP 水平的升高引起的，而不是像以前认为的那样由 AMP 引起的。AMPK 的激活依赖于其激活环上 Thr172 的 ADP 控制磷酸化，这是一种蛋白质调节机制，代表了变构调节修饰（ARM）的一个例子。AMPK 体现了阿特金森所设想的腺苷酸电荷调节系统的许多特征，其中合成代谢和分解代谢途径的调节受腺嘌呤核苷酸比值的调节。在这里，我们讨论了当前由腺嘌呤核苷酸调节 AMPK 的状态，并提出 AMPK 作为一种腺苷酸电荷调节蛋白激酶发挥作用。
