Department of Pathology, University of Cambridge, Cambridge CB2 1QP, England, UK.
J Cell Biol. 2010 Dec 27;191(7):1351-65. doi: 10.1083/jcb.201007060.
Cytokinesis, the final step of cell division, usually ends with the abscission of the two daughter cells. In some tissues, however, daughter cells never completely separate and remain interconnected by intercellular bridges or ring canals. In this paper, we report the identification and analysis of a novel ring canal component, Nessun Dorma (Nesd), isolated as an evolutionarily conserved partner of the centralspindlin complex, a key regulator of cytokinesis. Nesd contains a pectin lyase-like domain found in proteins that bind to polysaccharides, and we present evidence that it has high affinity for β-galactosides in vitro. Moreover, nesd is an essential gene in Drosophila melanogaster, in which it is required for completion of cytokinesis during male meiosis and possibly in female germline cells. Our findings indicate that Nesd is a novel carbohydrate-binding protein that functions together with centralspindlin in late cytokinesis, thus highlighting the importance of glycosylation in this process.
胞质分裂是细胞分裂的最后一步，通常以两个子细胞的分离结束。然而，在某些组织中，子细胞从未完全分离，而是通过细胞间桥或环道保持相互连接。在本文中，我们报告了一种新型环道成分 Nessun Dorma（Nesd）的鉴定和分析，它作为细胞分裂关键调节因子中心纺锤体复合物的一个进化保守的伴侣被分离出来。Nesd 包含一个在与多糖结合的蛋白质中发现的果胶裂解酶样结构域，我们提供的证据表明它在体外对β-半乳糖苷具有高亲和力。此外，nesd 是黑腹果蝇中的一个必需基因，在雄性减数分裂期间以及可能在雌性生殖细胞中完成胞质分裂时需要它。我们的发现表明，Nesd 是一种新型的碳水化合物结合蛋白，与中心纺锤体一起在胞质分裂的晚期发挥作用，从而突出了糖基化在这个过程中的重要性。
