Actomyosin networks are organized in space, direction, size, and connectivity to produce coordinated contractions across cells. We use the C. elegans spermatheca, a tube composed of contractile myoepithelial cells, to study how actomyosin structures are organized. FLN‐1/filamin is required for the formation and stabilization of a regular array of parallel, contractile, actomyosin fibers in this tissue. Loss of fln‐1 results in the detachment of actin fibers from the basal surface, which then accumulate along the cell junctions and are stabilized by spectrin. In addition, actin and myosin are captured at the nucleus by the linker of nucleoskeleton and cytoskeleton complex (LINC) complex, where they form large foci. Nuclear positioning and morphology, distribution of the endoplasmic reticulum and the mitochondrial network are also disrupted. These results demonstrate that filamin is required to prevent large actin bundle formation and detachment, to prevent excess nuclear localization of actin and myosin, and to ensure correct positioning of organelles.

中文翻译：

---

FLN-1/Filamin 需要锚定肌动球蛋白细胞骨架和收缩组织中亚细胞器的整体组织。

肌动球蛋白网络在空间、方向、大小和连通性上进行组织，以产生跨细胞的协调收缩。我们使用线虫受精囊（一种由收缩性肌上皮细胞组成的管）来研究肌动球蛋白结构的组织方式。FLN-1/细丝蛋白是在该组织中形成和稳定平行、收缩、肌动球蛋白纤维的规则阵列所必需的。fln-1丢失导致肌动蛋白纤维从基底表面脱离，然后沿着细胞连接处积聚并被血影蛋白稳定。此外，肌动蛋白和肌球蛋白被核骨架和细胞骨架复合物 (LINC) 复合物的接头捕获在细胞核处，在那里形成大的病灶。核定位和形态、内质网的分布和线粒体网络也被破坏。这些结果表明，需要细丝蛋白来防止大肌动蛋白束的形成和脱离，防止肌动蛋白和肌球蛋白的过度核定位，并确保细胞器的正确定位。