Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes.
Calcium/phospholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes.
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DOI：
10.1073/pnas.79.17.5249
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发表时间：
1982-09
影响因子：
11.1
通讯作者：
W. Wu;S. Walaas;A. Nairn;P. Greengard
中科院分区：
文献类型：
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作者：
W. Wu;S. Walaas;A. Nairn;P. Greengard
去极化诱导的钙离子流入大鼠大脑皮层突触体增加了几个突触体蛋白的磷酸化32 Pi掺入检查。涉及NaDodSO 4/聚丙烯酰胺凝胶的磷酸肽作图技术已被用于显示Mr 87，000底物蛋白的磷酸化受到去极化诱导的钙内流的刺激。磷酸化的这位先生87,000基板发生在突触体胞质溶胶和显着刺激钙/磷脂酰丝氨酸。钙调素抑制这种磷酸化反应。这种钙/磷脂依赖性蛋白激酶的底物富含神经元，并且似乎对神经元具有特异性。
Depolarization-induced calcium influx into rat cerebral cortex synaptosomes increased the phosphorylation of several synaptosomal proteins as examined by 32Pi incorporation. A phosphopeptide mapping technique involving NaDodSO4/polyacrylamide gels has been used to show that phosphorylation of a Mr 87,000 substrate protein is stimulated by depolarization-induced calcium influx. Phosphorylation of this Mr 87,000 substrate occurred in synaptosomal cytosol and was markedly stimulated by calcium/phosphatidylserine. Calmodulin inhibited this phosphorylation reaction. This substrate for calcium/phospholipid-dependent protein kinase is enriched in and appears to be specific to neurons.