AMP-activated protein kinase: nature's energy sensor
AMP-activated protein kinase: nature's energy sensor
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DOI：
10.1038/nchembio.610
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发表时间：
2011-08-01
影响因子：
14.8
通讯作者：
Gamblin, Steven J.
中科院分区：
文献类型：
--
作者：
Carling, David;Mayer, Faith V.;Gamblin, Steven J.
维持足够的ATP水平（细胞能量的直接来源）对于所有活细胞的正常功能至关重要。因此，细胞需要平衡能量需求与供应的机制。在真核细胞中，AMP激活的蛋白激酶（AMPK）级联在这种稳态中起重要作用。AMPK通过ATP的下降（伴随ADP和AMP的上升）激活，这导致分解代谢途径的激活和合成代谢途径的抑制。在这里，我们回顾AMPK作为能量传感器的作用，并考虑最近的发现，ADP，以及AMP，导致哺乳动物AMPK的激活。我们还回顾了磷酸化AMPK结构研究的最新进展，提供了一种调节AMPK的机制，其中AMP和ADP保护它免受去磷酸化。最后，我们简要地调查了一些悬而未决的问题有关的监管AMPK。
Maintaining sufficient levels of ATP (the immediate source of cellular energy) is essential for the proper functioning of all living cells. As a consequence, cells require mechanisms to balance energy demand with supply. In eukaryotic cells the AMP-activated protein kinase (AMPK) cascade has an important role in this homeostasis. AMPK is activated by a fall in ATP (concomitant with a rise in ADP and AMP), which leads to the activation of catabolic pathways and the inhibition of anabolic pathways. Here we review the role of AMPK as an energy sensor and consider the recent finding that ADP, as well as AMP, causes activation of mammalian AMPK. We also review recent progress in structural studies on phosphorylated AMPK that provides a mechanism for the regulation of AMPK in which AMP and ADP protect it against dephosphorylation. Finally, we briefly survey some of the outstanding questions concerning the regulation of AMPK.