KASH proteins in the outer nuclear membrane comprise the cytoplasmic half of LINC complexes that connect nuclei to the cytoskeleton. Caenorhabditis elegans ANC-1, an ortholog of Nesprin-1/2, contains actin-binding and KASH domains at opposite ends of a long spectrin-like region. Deletion of either the KASH or calponin homology (CH) domains does not completely disrupt nuclear positioning, suggesting neither KASH nor CH domains are essential. Deletions in the spectrin-like region of ANC-1 led to significant defects, but only recapitulated the null phenotype in combination with mutations in the trans-membrane span. In anc-1 mutants, the ER was unanchored, moving throughout the cytoplasm, and often fragmented. The data presented here support a cytoplasmic integrity model where ANC-1 localizes to the ER membrane and extends into the cytoplasm to position nuclei, ER, mitochondria, and likely other organelles in place.

中文翻译：

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Nesprin-1 / -2直系同源物ANC-1调节线虫中没有其KASH或肌动蛋白结合域的细胞器位置

外核膜中的KASH蛋白质包含LINC复合物的胞质半部，它们将核连接到细胞骨架。秀丽隐杆线虫ANC-1是Nesprin-1 / 2的直系同源物，在长的血影蛋白样区域的相对末端包含肌动蛋白结合域和KASH域。删除KASH或钙还原蛋白同源（CH）域不会完全破坏核定位，这表明KASH和CH域都不是必不可少的。ANC-1的血影蛋白样区域中的删除导致重大缺陷，但只概括了无效表型与跨膜跨度中的突变相结合。在anc-1突变体中，ER未锚定，在整个细胞质中移动，并经常断裂。