A COMMON BICYCLIC PROTEIN-KINASE CASCADE INACTIVATES THE REGULATORY ENZYMES OF FATTY-ACID AND CHOLESTEROL-BIOSYNTHESIS
A COMMON BICYCLIC PROTEIN-KINASE CASCADE INACTIVATES THE REGULATORY ENZYMES OF FATTY-ACID AND CHOLESTEROL-BIOSYNTHESIS
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DOI：
10.1016/0014-5793(87)80292-2
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发表时间：
1987-11-02
期刊：
影响因子：
3.5
通讯作者：
HARDIE, DG
中科院分区：
文献类型：
--
作者：
CARLING, D;ZAMMIT, VA;HARDIE, DG
一种高度纯化的大鼠肝脏蛋白激酶磷酸化并灭活乙酰辅酶A羧化酶，并在MgATP存在下导致微粒体HMG辅酶A还原酶快速灭活。这两种作用都以相同的方式刺激AMP，并大大降低了事先处理的激酶与纯化的蛋白磷酸酶。去磷酸化的激酶可以在MgATP存在下重新激活，显然是由于不同的激酶激酶，并且这种重新激活由纳摩尔浓度的棕榈酰辅酶A刺激。这些结果表明，一个共同的双环蛋白激酶级联可以有效地抑制脂肪酸和胆固醇生物合成的调节酶。
A highly purified rat liver protein kinase phosphorylates and inactivates acetyl‐CoA carboxylase, and causes rapid inactivation of microsomal HMG‐CoA reductase in the presence of MgATP. Both effects are stimulated in an identical manner by AMP, and are greatly reduced by prior treatment of the kinase with purified protein phosphatase. The dephosphorylated kinase can be reactivated in the presence of MgATP, apparently due to a distinct kinase kinase, and this reactivation is stimulated by nanomolar concentrations of palmitoyl‐CoA. These results show that a common, bicyclic protein kinase cascade can potently inactivate the regulatory enzymes of both fatty acid and cholesterol biosynthesis.