Wrenn R W, Katoh N, Wise B C, Kuo J F
J Biol Chem. 1980 Dec 25;255(24):12042-6.
The Ca2+-dependent phosphorylation of a number of proteins in the cytosol of the rat or guinea pig cerebral cortex was profoundly stimulated by phosphatidylserine; calmodulin, on the other hand, had only a minimal effect. The Ca2+-dependent phosphorylation of different proteins from the total particulate fraction of the same tissue, in comparison, was specifically stimulated by either phosphatidylserine or calmodulin. The present findings, in line with the phospholipid-sensitive Ca2+-dependent protein kinase recently recognized, suggest an involvement of phospholipid in regulating Ca2+-dependent phosphorylation of endogenous substrate proteins. This new system presumably functions independent or in a complementary manner with the calmodulin-sensitive Ca2+-dependent protein phosphorylation system previously reported by others.
磷脂酰丝氨酸可显著刺激大鼠或豚鼠大脑皮质细胞质中多种蛋白质的钙依赖性磷酸化；另一方面，钙调蛋白的作用微乎其微。相比之下，同一组织总颗粒部分中不同蛋白质的钙依赖性磷酸化则受到磷脂酰丝氨酸或钙调蛋白的特异性刺激。目前的研究结果与最近发现的对磷脂敏感的钙依赖性蛋白激酶一致，表明磷脂参与调节内源性底物蛋白的钙依赖性磷酸化。这个新系统可能独立发挥作用，或以互补方式与其他人先前报道的对钙调蛋白敏感的钙依赖性蛋白磷酸化系统共同发挥作用。
