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Constricting membranes at the nano and micro scale

机译:纳米和微米级收缩膜

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摘要

Dynamin GTPases regulate membrane traffic, in part, by constricting nanometer-sized membrane tubes to form vesicles by fission. In this issue of PNAS, Chua et al. (1) report that dynamin2 remodels membranes on a much grander scale by influencing the contractile activity of actomyosin encircling epithelial cells at their apical cell-cell junctions. Using a simple epithelial cell system, Madin-Darby canine kidney (MDCK) epithelial cells, Chua et al. found that apical junctional complexes that contain the cytoskeletal linker protein, ZO-1, and elements of the basolat-eral F-actin cytoskeleton, were missing or poorly organized in cells depleted of dynamin2. Notably, in MDCK cells expressing the GTP-binding-defective mutant protein, dynamin2-K44A, polarized membrane domains defined by ZO-1-containing apical junctions formed, but the circumferential actomyosin network associated with junctional complexes was constricted > 2-fold over that in cells expressing wild-type dynamin2 (Fig. 1).
机译:Dynamin GTPases部分地通过收缩纳米尺寸的膜管以通过裂变形成囊泡来调节膜的运输。在本期PNAS中,Chua等人。 (1)报告说,dynamin2通过影响围绕在顶部细胞-细胞连接处的上皮细胞的放线菌素的收缩活性,在更大范围内重塑膜。使用简单的上皮细胞系统,Madin-Darby犬肾(MDCK)上皮细胞,Chua等。发现,在含有dynamin2的细胞中,含有细胞骨架接头蛋白ZO-1和杆状细菌F-肌动蛋白细胞骨架成分的根尖连接复合物缺失或组织不良。值得注意的是,在表达GTP结合缺陷型突变蛋白dynamin2-K44A的MDCK细胞中,形成了由含ZO-1的顶端连接所定义的极化膜结构域,但与连接复合物相关的周生肌球蛋白网络被压缩了2倍以上。表达野生型dynamin2的细胞中的表达(图1)。

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