AMP-activated protein kinase: also regulated by ADP?

被引:148
作者
Hardie, D. Grahame [1 ]
Carling, David [2 ]
Gamblin, Steven J. [3 ]
机构
[1] Univ Dundee, Coll Life Sci, Dundee DD1 5EH, Scotland
[2] Univ London Imperial Coll Sci Technol & Med, MRC Clin Sci Ctr, London W12 0NN, England
[3] MRC Natl Inst Med Res, London NW7 1AA, England
基金
英国惠康基金; 英国医学研究理事会;
关键词
SACCHAROMYCES-CEREVISIAE; UPSTREAM KINASE; SKELETAL-MUSCLE; RAT-LIVER; 3-HYDROXY-3-METHYLGLUTARYL COENZYME; ENCEPHALITOZOON-CUNICULI; REDUCTASE KINASE; STRUCTURAL BASIS; KEY REGULATOR; YEAST SNF1;
D O I
10.1016/j.tibs.2011.06.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 beta subunit and the mechanisms by which it is activated by drugs and xenobiotics such as metformin and resveratrol.
引用
收藏
页码:470 / 477
页数:8
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