Department of Protein Chemistry and Metabolism, St. Vincent's Institute of Medical Research, University of Melbourne, 41 Victoria Parade, Fitzroy 3065, Victoria, Australia.
Science. 2011 Jun 17;332(6036):1433-5. doi: 10.1126/science.1200094.
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.
腺苷一磷酸（AMP）激活的蛋白激酶（AMPK）通过响应能量需求和供应来调节全身和细胞能量平衡。AMPK 是一种由三磷酸腺苷（ATP）浓度降低和 AMP 浓度增加激活的αβγ异三聚体。AMPK 的激活依赖于激酶 LKB1 或 CaMKKβ对α催化亚基苏氨酸-172（Thr(172)）的磷酸化，这是由 AMP 结合到γ亚基促进的。AMP 通过抑制α-Thr(172)的去磷酸化来维持活性，而 ATP 则促进去磷酸化。二磷酸腺苷（ADP）与 γ 位点 1 和 3结合，类似于 AMP，并刺激α-Thr(172)磷酸化。然而，与 AMP 不同的是，ADP 并没有直接激活磷酸化的 AMPK。通过这种方式，ADP/ATP 和 AMP/ATP 比值都有助于 AMPK 的调节。
