Gschwendt M, Kittstein W, Marks F
German Cancer Research Center, Heidelberg.
FEBS Lett. 1994 Jan 24;338(1):85-8. doi: 10.1016/0014-5793(94)80121-5.
The elongation factor-2 (eEF-2) is selectively phosphorylated by the eEF-2 kinase (calmodulin-dependent kinase III). This phosphorylation can be inhibited by calmodulin antagonists, such as CGS 9343B (IC50 = 4 microM). The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylation with an IC50 of 5.3 microM. By contrast, the eEF-2 kinase is rather resistant towards the potent but non-selective protein kinase inhibitor staurosporine (IC50 > 50 microM) and thus can be differentiated from most other protein kinases that are suppressed by staurosporine in the nM range.
延伸因子2（eEF-2）被eEF-2激酶（钙调蛋白依赖性激酶III）选择性磷酸化。这种磷酸化可被钙调蛋白拮抗剂如CGS 9343B（IC50 = 4 microM）抑制。新型蛋白激酶抑制剂rottlerin显示出以5.3 microM的IC50抑制eEF-2磷酸化。相比之下，eEF-2激酶对强效但非选择性的蛋白激酶抑制剂星形孢菌素相当耐药（IC50 > 50 microM），因此可以与大多数其他在纳摩尔范围内被星形孢菌素抑制的蛋白激酶区分开来。
