Schindler M, Jiang L W
J Cell Biol. 1986 Mar;102(3):859-62. doi: 10.1083/jcb.102.3.859.
Fluorescence redistribution after photobleaching (FRAP) was used to examine the role of actin and myosin in the transport of dextrans through the nuclear pore complex. Anti-actin antibodies added to isolated rat liver nuclei significantly reduced the flux rate of fluorescently labeled 64-kD dextrans. The addition of 3 mM ATP to nuclei, which enhances the flux rate in control nuclei by approximately 250%, had no enhancement effect in the presence of either anti-actin or anti-myosin antibody. Phalloidin (10 microM) and cytochalasin D (1 micrograms/ml) individually inhibited the ATP stimulation of transport. Rabbit serum, anti-fibronectin, and anti-lamins A and C antibodies had no effect on transport. These results suggest a model for nuclear transport in which actin/myosin are involved in an ATP-dependent process that alters the effective transport rate across the nuclear pore complex.
采用光漂白后的荧光再分布（FRAP）技术来研究肌动蛋白和肌球蛋白在葡聚糖通过核孔复合体运输过程中的作用。向分离出的大鼠肝细胞核中添加抗肌动蛋白抗体，可显著降低荧光标记的64-kD葡聚糖的通量率。向细胞核中添加3 mM ATP可使对照细胞核中的通量率提高约250%，但在存在抗肌动蛋白或抗肌球蛋白抗体的情况下，这种增强作用消失。鬼笔环肽（10 microM）和细胞松弛素D（1微克/毫升）分别抑制了ATP对运输的刺激作用。兔血清、抗纤连蛋白以及抗核纤层蛋白A和C抗体对运输没有影响。这些结果提示了一种核运输模型，其中肌动蛋白/肌球蛋白参与了一个依赖ATP的过程，该过程改变了跨核孔复合体的有效运输速率。
