Inhibitory effect of calmodulin on phosphorylation of NAP-22 with protein kinase C.
Inhibitory effect of calmodulin on phosphorylation of NAP-22 with protein kinase C.
复制标题
钙调蛋白对 NAP-22 与蛋白激酶 C 磷酸化的抑制作用。
DOI：
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发表时间：
1994
影响因子：
4.8
通讯作者：
S. Nakamura
中科院分区：
文献类型：
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作者：
S. Maekawa;H. Murofushi;S. Nakamura
NAP-22 是最近发现的一种富含神经组织的酸性蛋白，在体外被证明是蛋白激酶 C 的底物。使用大肠杆菌中表达的缺失突变体将其磷酸化位点指定为 Ser6。钙调蛋白抑制这种磷酸化反应。钙调蛋白的这种抑制作用是剂量依赖性的，并且比其对蛋白激酶C对神经调节蛋白（GAP-43）磷酸化的抑制作用强得多。利用丹磺酰标记的钙调蛋白的荧光变化获得的NAP-22和钙调蛋白的解离常数远低于神经调节蛋白和钙调蛋白的解离常数。 NAP-22 的磷酸化抑制了与钙调蛋白的结合。
NAP-22, a recently identified neural tissue-enriched acidic protein, was shown to be a substrate of protein kinase C in vitro. Its phosphorylation site was assigned as Ser6 using deleted mutants expressed in Escherichia coli. Calmodulin inhibited this phosphorylation reaction. This inhibitory effect of calmodulin was dose-dependent and much stronger than its inhibitory effect to the phosphorylation of neuromodulin (GAP-43) with protein kinase C. The dissociation constant of NAP-22 and calmodulin obtained using the fluorescence change of dansyl-labeled calmodulin was much lower than that of neuromodulin and calmodulin. The phosphorylation of NAP-22 inhibited the association with calmodulin.