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腺苷酸活化蛋白激酶:也受 ADP 调节?

AMP-activated protein kinase: also regulated by ADP?

机构信息

College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.

出版信息

Trends Biochem Sci. 2011 Sep;36(9):470-7. doi: 10.1016/j.tibs.2011.06.004. Epub 2011 Jul 23.

DOI:10.1016/j.tibs.2011.06.004
PMID:21782450
Abstract

AMPK is a ubiquitous sensor of cellular energy status in eukaryotic cells. It is activated by stresses causing ATP depletion and, once activated, maintains energy homeostasis by phosphorylating targets that activate catabolism and inhibit energy-consuming processes. Evidence derived from non-mammalian orthologs suggests that its ancestral role was in the response to starvation for a carbon source. We review recent findings showing that AMPK is activated by ADP as well as AMP, and discuss the mechanism by which binding of these nucleotides prevent its dephosphorylation and inactivation. We also discuss the role of the carbohydrate-binding module on the β subunit and the mechanisms by which it is activated by drugs and xenobiotics such as metformin and resveratrol.

摘要

AMPK 是真核细胞中细胞能量状态的普遍传感器。它通过导致 ATP 消耗的应激激活,一旦被激活,通过磷酸化激活分解代谢和抑制耗能过程的靶标来维持能量稳态。源自非哺乳动物直系同源物的证据表明,其祖先的作用是对碳源饥饿的反应。我们综述了最近的发现,表明 AMPK 可被 ADP 和 AMP 激活,并讨论了结合这些核苷酸防止其去磷酸化和失活的机制。我们还讨论了碳水化合物结合模块在β亚基上的作用以及它如何被二甲双胍和白藜芦醇等药物和外源性化学物质激活的机制。

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