The nuclear envelope protein nesprin‐2G is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex and is responsible for mechanical and signaling crosstalk between the nucleus and cytoskeleton. A prior study has demonstrated that nesprin‐2G knockout mice show delayed wound healing. The goal was to elucidate the mechanism underlying the delayed wound closure in this mouse model. Primary fibroblasts from wild‐type and knockout neonatal mice were isolated. Knockout cells exhibited decreased focal adhesion (FA) size, number, and intensity. Consistent with this result, FA protein expression levels were decreased in knockout cells. Additionally, knockout fibroblasts displayed an abnormal actin cytoskeleton, as evidenced by loss of TAN line formation and both cytoplasmic and peri‐nuclear actin staining. Using collective and single cell motility assays, it was found that knockout cells exhibited a reduction in both speed and directed migration. Traction force microscopy revealed that knockout fibroblasts generated fewer traction forces compared with WT fibroblasts. In summary, the data indicated that changes in actin organization and defects in FAs result in a reduced ability of knockout fibroblasts to generate traction forces needed for efficient motility.

中文翻译：

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Nesprin-2G敲除成纤维细胞显示出减少的迁移，粘着斑成分的变化以及产生牵引力的能力降低。

核被膜蛋白nesprin-2G是核骨架和细胞骨架（LINC）复合体的连接子的一个组成部分，负责核与细胞骨架之间的机械和信号串扰。先前的研究表明，nesprin-2G基因敲除小鼠显示伤口愈合延迟。目的是阐明该小鼠模型中延迟伤口闭合的机制。从野生型和基因敲除的新生小鼠中分离出原代成纤维细胞。敲除细胞表现出减少的粘着斑（FA）大小，数量和强度。与该结果一致，基因敲除细胞中FA蛋白表达水平降低。此外，敲除的成纤维细胞显示出异常的肌动蛋白细胞骨架，这由TAN系形成的丧失以及细胞质和核周肌动蛋白染色所证明。使用集体和单细胞运动性测定，发现敲除细胞在速度和定向迁移上均表现出降低。牵引力显微镜显示，与野生型成纤维细胞相比，基因敲除的成纤维细胞产生的牵引力更小。总之，数据表明肌动蛋白组织的变化和FA的缺陷导致基因敲除的成纤维细胞产生有效运动所需的牵引力的能力降低。