Substrate specificity of Ca2+/CaM-dependent multifunctional protein kinases: comparison of isoenzymes from brain, liver and skeletal muscle.

Substrate specificity of Ca2+/CaM-dependent multifunctional protein kinases: comparison of isoenzymes from brain, liver and skeletal muscle.
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Ca2/CaM 依赖性多功能蛋白激酶的底物特异性:来自脑、肝脏和骨骼肌的同工酶的比较。

DOI:
10.1016/s0006-291x(88)80508-4
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发表时间:
1988
影响因子:
3.1
通讯作者:
Kelly,PT
Kelly,PT
中科院分区:
生物学4区
文献类型:
--
作者:
Shenolikar,S;Langston,J;Schworer,CM;Kelly,PT

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通过对多种蛋白质底物的磷酸化,比较了脑、骨骼肌和肝脏中依赖于钙/钙调素的多功能蛋白激酶同工酶。在本实验条件下,三种同工酶均表现出突触素I和糖原合成酶的快速磷酸化。相比之下,丙酮酸激酶和苯丙氨酸羟基酶的磷酸化速度几乎慢了两个数量级。后两种底物的特异性磷酸化也在三种蛋白激酶之间观察到差异。钙/钙调素依赖性蛋白激酶的磷酸化与cAMP依赖性蛋白激酶的磷酸化形成对比,cAMP依赖性蛋白激酶在体外和体内都使这些蛋白磷酸化。讨论了钙/钙调素依赖的多功能蛋白激酶在这些底物的钙依赖的磷酸化中的潜在作用。
Ca2+/CaM-dependent multifunctional protein kinase isoenzymes from brain, skeletal muscle and liver were compared by their phosphorylation of a number of protein substrates. Under the conditions of assay, the three isoenzymes demonstrated rapid phosphorylation of synapsin I and glycogen synthase. In contrast, rates of phosphorylation of pyruvate kinase and phenylalanine hydroxylase were almost two orders of magnitude slower. Differences in phosphorylation specifically of the latter two substrates was also observed among the three protein kinases. Phosphorylation by Ca2+/CaM-dependent protein kinases was contrasted with cAMP-dependent protein kinase, which phosphorylates these proteinsin vitroandin vivo. The potential role of Ca2+/CaM-dependent multifunctional protein kinases in the Ca2+-dependent phosphorylation of these substrates is discussed.
DOI: 10.1111/j.1432-1033.1986.tb10502.x
发表时间: 1986
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