Sensing and responding to energetic stress: Evolution of the AMPK network
Sensing and responding to energetic stress: Evolution of the AMPK network
复制标题
DOI：
10.1016/j.cbpb.2017.11.001
复制
发表时间：
2018-10-01
影响因子：
2.2
通讯作者：
LeMoine, Christophe M. R.
中科院分区：
文献类型：
--
作者：
Craig, Paul M.;Moyes, Christopher D.;LeMoine, Christophe M. R.
AMP活化蛋白激酶是一种介导细胞能量状态与多种效应蛋白之间通讯的酶，特别是那些在决定代谢表型中发挥作用的效应蛋白。通过磷酸化参与细胞结构的代谢酶、转录调节因子和蛋白质，它可以在短期和长期内改变能量代谢。它的基本特征是高度保守的，在所有真核生物中都有同源物。基因和/或基因组复制赋予早期脊椎动物AMPK亚基的旁系同源物，尽管其亚功能化的性质仍然不确定，即使在哺乳动物中也是如此。虽然大多数研究集中在酶在人类健康中的作用，但可以从针对非传统模型动物的比较研究中学到很多东西。特别是鱼类，是有趣的模型，因为代谢特性的多样性和代谢与环境挑战之间的复杂关系。在这篇综述中，我们通过比较生理学的透镜来研究AMPK的结构和功能，寻找机会更好地了解这种生命能量传感器在动物中的进化。
AMP-activated protein kinase is an enzyme that mediates communication between cellular energy status and diverse effector proteins, particularly those that play roles in determining the metabolic phenotype. By phosphorylating metabolic enzymes, transcriptional regulators and proteins involved in cellular structure, it can modify energy metabolism in both the short term and long term. Its basic features are highly conserved, with homologues in all eukaryotes. Gene and/or genome duplications endowed early vertebrates with paralogs of AMPK subunits, though the nature of their subfunctionalization remains uncertain, even in mammals. While most research focuses on the role of the enzyme in human health, a great deal can be learned from comparative studies targeting non-traditional model animals. Fish, in particular, are interesting models because of the diversity in the metabolic properties and complex relationships between metabolism and environmental challenges. In this review, we examine what is known about AMPK structure and function though the lens of comparative physiology, looking for opportunities to better understand how this vital energy sensor has evolved in animals.