Phosphorylation and associated translocation of the 87-kDa protein, a major protein kinase C substrate, in isolated nerve terminals.
Phosphorylation and associated translocation of the 87-kDa protein, a major protein kinase C substrate, in isolated nerve terminals.
复制标题
分离神经末梢中 87-kDa 蛋白（一种主要蛋白激酶 C 底物）的磷酸化和相关易位。
DOI：
10.1073/pnas.86.7.2253
复制
发表时间：
1989
影响因子：
11.1
通讯作者：
Greengard,P
中科院分区：
文献类型：
--
作者：
Wang,JK;Walaas,SI;Sihra,TS;Aderem,A;Greengard,P
87千道尔顿（87 kDa）的蛋白质先前被鉴定为神经元和其他组织中蛋白激酶C的主要特异性底物。我们现在已经研究了蛋白激酶C催化的磷酸化的这种蛋白质的影响，其与膜在分离的神经末梢（突触体）从大鼠大脑皮层。在与蛋白激酶C激活相关的条件下孵育突触体膜导致磷酸化的87-kDa蛋白释放到孵育介质中。在完整的突触体中，蛋白激酶C的激活佛波酯或去极化诱导的Ca 2+内流引起的87-kDa蛋白的磷酸化增加，其从膜到胞质溶胶的易位。这种易位表现出时间进程，钙依赖性，和可逆性类似的观察到的蛋白激酶C诱导的蛋白磷酸化。这些结果表明，蛋白激酶C催化的磷酸化的87 kDa的蛋白是负责其亚细胞易位到神经末梢的胞质溶胶。
A protein of 87 kilodaltons (87 kDa) was previously identified as a major specific substrate for protein kinase C in neuronal and other tissues. We have now studied the effect of protein kinase C-catalyzed phosphorylation of this protein on its association with membranes in isolated nerve terminals (synaptosomes) from rat cerebral cortex. Incubation of synaptosomal membranes under conditions associated with activation of protein kinase C led to the release of the phosphorylated 87-kDa protein into the incubation medium. In intact synaptosomes, activation of protein kinase C by phorbol esters or by depolarization-induced Ca2+ influx caused an increased phosphorylation of the 87-kDa protein and its translocation from membrane to cytosol. This translocation showed time courses, calcium dependency, and reversibility similar to those observed for the protein kinase C-induced phosphorylation of the protein. These results suggest that protein kinase C-catalyzed phosphorylation of the 87-kDa protein is responsible for its subcellular translocation into the cytosol of nerve terminals.