AMPK Is a Direct Adenylate Charge-Regulated Protein Kinase

被引：457

作者：

Oakhill, Jonathan S. ^{[1
]}

Steel, Rohan ^{[1
]}

Chen, Zhi-Ping ^{[1
]}

Scott, John W. ^{[1
]}

Ling, Naomi ^{[1
]}

Tam, Shanna ^{[1
]}

Kemp, Bruce E. ^{[1
]}

机构：

[1] Univ Melbourne, St Vincents Inst Med Res, Dept Prot Chem & Metab, Fitzroy, Vic 3065, Australia

来源：

SCIENCE | 2011年 / 332卷 / 6036期

基金：

英国医学研究理事会; 澳大利亚研究理事会;

关键词：

NUCLEAR-MAGNETIC-RESONANCE; ACETYL-COA CARBOXYLASE; SKELETAL-MUSCLE; ENERGY-CHARGE; 3-HYDROXY-3-METHYLGLUTARYL-COA REDUCTASE; ADP; PHOSPHORYLATION; INACTIVATION; METABOLISM; EXERCISE;

D O I：

10.1126/science.1200094

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

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 alpha beta gamma heterotrimer activated by decreasing concentrations of adenosine triphosphate (ATP) and increasing AMP concentrations. AMPK activation depends on phosphorylation of the alpha catalytic subunit on threonine-172 (Thr(172)) by kinases LKB1 or CaMKK beta, and this is promoted by AMP binding to the gamma subunit. AMP sustains activity by inhibiting dephosphorylation of alpha-Thr(172), whereas ATP promotes dephosphorylation. Adenosine diphosphate (ADP), like AMP, bound to gamma sites 1 and 3 and stimulated alpha-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.

引用

页码：1433 / 1435

页数：3

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