INTERACTION OF PROTEIN-KINASE-C WITH PHOSPHATIDYLSERINE .2. SPECIFICITY AND REGULATION
INTERACTION OF PROTEIN-KINASE-C WITH PHOSPHATIDYLSERINE .2. SPECIFICITY AND REGULATION
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DOI：
10.1021/bi00134a019
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发表时间：
1992-05-19
期刊：
影响因子：
2.9
通讯作者：
NEWTON, AC
中科院分区：
文献类型：
--
作者：
ORR, JW;NEWTON, AC
特异性和非特异性相互作用在脂类调节蛋白激酶C中的作用已经被研究。结合和活性测量揭示了蛋白激酶C与膜相互作用的两种机制：(1)与激活的磷脂酰丝氨酸特异性结合；(2)与非活化的酸性脂质的非特异性结合。与磷脂酰丝氨酸的特异性相互作用对离子强度、表面电荷和非活化脂的存在相对不敏感。该蛋白的两个第二信使--甘油二酯和钙离子显著增加了该蛋白对磷脂酰丝氨酸的亲和力。相反，非特异性相互作用对离子强度和表面电荷很敏感，不受二酰基甘油的影响。这些结果表明，静电相互作用促进了蛋白激酶C与膜的结合，但磷脂酰丝氨酸的协同和选择性结合是产生蛋白质-脂质相互作用的主要驱动力。
The roles of specific and nonspecific interactions in the regulation of protein kinase C by lipid have been examined. Binding and activity measurements reveal two mechanisms by which protein kinase C interacts with membranes: (1) a specific binding to the activating lipid phosphatidylserine and (2) a nonspecific binding to nonactivating, acidic lipids. The specific interaction with phosphatidylserine is relatively insensitive to ionic strength, surface charge, and the presence of nonactivating lipids. The two second messengers of the kinase, diacylglycerol and Ca2+, increase markedly the affinity of the kinase for phosphatidylserine. In contrast, the nonspecific interaction is sensitive to ionic strength and surface charge, and is unaffected by diacylglycerol. These results suggest that electrostatic interactions promote the binding of protein kinase C to membranes but the cooperative and selective binding of phosphatidylserine is the dominant driving force in a productive protein-lipid interaction.