The formins Cdc12 and For3 cooperate during contractile ring assembly in cytokinesis
The formins Cdc12 and For3 cooperate during contractile ring assembly in cytokinesis
复制标题
DOI：
10.1083/jcb.201305022
复制
发表时间：
2013-10-14
影响因子：
7.8
通讯作者：
Wu, Jian-Qiu
中科院分区：
文献类型：
--
作者：
Coffman, Valerie C.;Sees, Jennifer A.;Wu, Jian-Qiu
在分裂位点重新组装的肌动蛋白丝和通过定向皮质运输募集的现有丝都有助于细胞分裂过程中收缩环的形成。然而，目前尚不清楚哪个来源更重要。在这里，我们发现裂变酵母formin For3在缺乏formin Cdc12的情况下负责节点凝结成团块。For3在分裂位点的定位取决于F-BAR蛋白Cdc15， For3的缺失是合成致死性的，突变会导致收缩环形成缺陷。For3在表达Cdc12 n端截断的细胞中变得至关重要，Cdc12在肌动蛋白组装中更活跃，但依赖于肌动蛋白丝定位到分裂位点。在四分体荧光显微镜下，for3缺失和cdc12截断的双突变体在收缩环组装和收缩方面存在严重缺陷，尽管肌动蛋白丝的皮质运输正常。综上所述，这些数据表明不同的形成蛋白在细胞分裂过程中相互合作，并且在分裂位点的新生肌动蛋白组装在收缩环形成中占主导地位。
Both de novo assembled actin filaments at the division site and existing filaments recruited by directional cortical transport contribute to contractile ring formation during cytokinesis. However, it is unknown which source is more important. Here, we show that fission yeast formin For3 is responsible for node condensation into clumps in the absence of formin Cdc12. For3 localization at the division site depended on the F-BAR protein Cdc15, and for3 deletion was synthetic lethal with mutations that cause defects in contractile ring formation. For3 became essential in cells expressing N-terminal truncations of Cdc12, which were more active in actin assembly but depended on actin filaments for localization to the division site. In tetrad fluorescence microscopy, double mutants of for3 deletion and cdc12 truncations were severely defective in contractile ring assembly and constriction, although cortical transport of actin filaments was normal. Together, these data indicate that different formins cooperate in cytokinesis and that de novo actin assembly at the division site is predominant for contractile ring formation.