Casella J F, Craig S W, Maack D J, Brown A E
J Cell Biol. 1987 Jul;105(1):371-9. doi: 10.1083/jcb.105.1.371.
Various biological activities have been attributed to actin-capping proteins based on their in vitro effects on actin filaments. However, there is little direct evidence for their in vivo activities. In this paper, we show that Cap Z(36/32), a barbed end, actin-capping protein isolated from muscle (Casella, J. F., D. J. Maack, and S. Lin, 1986, J. Biol. Chem., 261:10915-10921) is localized to the barbed ends of actin filaments by electron microscopy and to the Z-line of chicken skeletal muscle by indirect immunofluorescence and electron microscopy. Since actin filaments associate with the Z-line at their barbed ends, these findings suggest that Cap Z(36/32) may play a role in regulating length, orienting, or attaching actin filaments to Z-discs.
基于肌动蛋白封端蛋白对肌动蛋白丝的体外作用,人们赋予了它们多种生物学活性。然而,几乎没有直接证据证明它们在体内的活性。在本文中,我们发现Cap Z(36/32),一种从肌肉中分离出来的位于肌动蛋白丝尖端的封端蛋白(Casella, J. F., D. J. Maack, and S. Lin, 1986, J. Biol. Chem., 261:10915 - 10921),通过电子显微镜观察定位于肌动蛋白丝的尖端,通过间接免疫荧光和电子显微镜观察定位于鸡骨骼肌的Z线。由于肌动蛋白丝在其尖端与Z线相连,这些发现表明Cap Z(36/32)可能在调节肌动蛋白丝长度、使其定向或将其附着于Z盘方面发挥作用。