脱磷
腺苷酸激酶
安普克
蛋白激酶A
一磷酸腺苷
三磷酸腺苷
磷酸化
能量电荷
腺苷
AMP活化蛋白激酶
二磷酸腺苷
化学
生物化学
激酶
细胞生物学
磷酸酶
生物
酶
血小板
免疫学
血小板聚集
作者
Jonathan S. Oakhill,Rohan Steel,Zhiping Chen,John W. Scott,Naomi X.Y. Ling,Shanna Tam,Bruce E. Kemp
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2011-06-16
卷期号:332 (6036): 1433-1435
被引量:504
标识
DOI:10.1126/science.1200094
摘要
The adenosine monophosphate (AMP)-activated protein kinase (AMPK) regulates whole-body and cellular energy balance in response to energy demand and supply. AMPK is an αβγ heterotrimer activated by decreasing concentrations of adenosine triphosphate (ATP) and increasing AMP concentrations. AMPK activation depends on phosphorylation of the α catalytic subunit on threonine-172 (Thr(172)) by kinases LKB1 or CaMKKβ, and this is promoted by AMP binding to the γ subunit. AMP sustains activity by inhibiting dephosphorylation of α-Thr(172), whereas ATP promotes dephosphorylation. Adenosine diphosphate (ADP), like AMP, bound to γ sites 1 and 3 and stimulated α-Thr(172) phosphorylation. However, in contrast to AMP, ADP did not directly activate phosphorylated AMPK. In this way, both ADP/ATP and AMP/ATP ratios contribute to AMPK regulation.
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