Friederich E, Huet C, Arpin M, Louvard D
Institut Pasteur, Département de Biologie Moléculaire, Paris, France.
Cell. 1989 Nov 3;59(3):461-75. doi: 10.1016/0092-8674(89)90030-5.
The function of villin, an actin-binding protein, has been investigated by transfecting fibroblasts with cloned human cDNAs encoding wild-type villin or functional villin domains. Synthesis of large amounts of villin induced the growth of numerous long microvilli on cell surfaces together with the redistribution of F-actin. These microvilli contained a cytoskeleton of F-actin, and their appearance was frequently accompanied by the disappearance of stress fibers. The complete villin gene sequence was required to exert its morphogenic effect. Villin lacking one actin-binding domain (113 amino acids), located at its carboxyterminal end, did not induce growth if microvilli or stress fiber disruption. Our results indicate that villin plays a key role in vivo in the morphogenesis of microvilli.
肌动蛋白结合蛋白绒毛蛋白的功能已通过用编码野生型绒毛蛋白或功能性绒毛蛋白结构域的克隆人cDNA转染成纤维细胞进行了研究。大量绒毛蛋白的合成诱导了细胞表面大量长微绒毛的生长以及F-肌动蛋白的重新分布。这些微绒毛含有F-肌动蛋白细胞骨架，其出现常常伴随着应力纤维的消失。发挥其形态发生作用需要完整的绒毛蛋白基因序列。缺少位于其羧基末端的一个肌动蛋白结合结构域（113个氨基酸）的绒毛蛋白不会诱导微绒毛生长或应力纤维破坏。我们的结果表明，绒毛蛋白在微绒毛的体内形态发生中起关键作用。
