Ito S, Richert N, Pastan I
Proc Natl Acad Sci U S A. 1982 Aug;79(15):4628-31. doi: 10.1073/pnas.79.15.4628.
The phosphorylation of vinculin by a highly purified tyrosine-specific protein kinase was enhanced more than 10-fold by anionic phospholipids: the phosphorylation of casein, actin, and alpha-actinin was inhibited. The effect of phospholipid was dependent on the divalent cation used. Stimulation was observed by phosphatidylinositol or phosphatidylglycerol in the presence of either 0.5 mM Mn2+ of 5 mM Mg2+; with either phospholipid, more enzyme activity was observed with Mn2+. Maximal stimulation by phosphatidylinositol was observed at about 400 micrograms/ml. In contrast, marked stimulation by phosphatidylserine was observed only with Mn2+ and marked stimulation by phosphatidic acid was observed only with Mg2+. These results raise the possibility that phospholipids modulate vinculin phosphorylation in Rous sarcoma virus-transformed cells.
一种高度纯化的酪氨酸特异性蛋白激酶对纽蛋白的磷酸化作用在阴离子磷脂存在时增强了10倍以上：而对酪蛋白、肌动蛋白和α-辅肌动蛋白的磷酸化作用则受到抑制。磷脂的作用取决于所使用的二价阳离子。在存在0.5 mM Mn2+ 或5 mM Mg2+ 的情况下，磷脂酰肌醇或磷脂酰甘油可观察到刺激作用；对于任何一种磷脂，在Mn2+ 存在时观察到更多的酶活性。磷脂酰肌醇在约400微克/毫升时观察到最大刺激作用。相比之下，仅在Mn2+ 存在时观察到磷脂酰丝氨酸的显著刺激作用，而仅在Mg2+ 存在时观察到磷脂酸的显著刺激作用。这些结果增加了磷脂调节劳氏肉瘤病毒转化细胞中纽蛋白磷酸化的可能性。
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