Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity
Characterization of anillin mutants reveals essential roles in septin localization and plasma membrane integrity
复制标题
DOI：
10.1242/dev.01843
复制
发表时间：
2005-06-01
期刊：
影响因子：
4.6
通讯作者：
Sullivan, W
中科院分区：
文献类型：
--
作者：
Field, CM;Coughlin, M;Sullivan, W
氨苄素是细胞分裂所必需的收缩环的保守成分，在生化分析中与三种保守的裂解沟蛋白F-actin， myosin11和septin相互作用。我们证明果蝇的废料基因，确定为一个基因参与细胞化，编码苯胺。我们描述了一系列母体效应和合子氨酰胺等位基因在细胞化、极细胞形成和细胞分裂方面的缺陷。突变导致氨苄素c端PH结构域的氨基酸改变，导致沟管和收缩环的septin募集缺陷。这些突变也强烈地扰乱了细胞化，改变了沟侵入的时间和速度。它们引起新质膜的剧烈囊泡，并破坏细胞质柄的稳定，细胞质柄通常连接原肠泌细胞和卵黄团。靠近N端的突变阻断了极细胞的分离，对细胞化的影响较小，突出了收缩过程之间的机制差异。综上所述，我们的数据表明Anillin在支架裂解沟组分、直接稳定细胞内桥和间接稳定细胞化过程中新沉积的质膜中的重要作用。
Anillin is a conserved component of the contractile ring that is essential for cytokinesis, and physically interacts with three conserved cleavage furrow proteins, F-actin, myosin 11 and septins in biochemical assays. We demonstrate that the Drosophila scraps gene, identified as a gene involved in cellularization, encodes Anillin. We characterize defects in cellularization, pole cell formation and cytokinesis in a series of maternal effect and zygotic anillin alleles. Mutations that result in amino acid changes in the C-terminal PH domain of Anillin cause defects in septin recruitment to the furrow canal and contractile ring. These mutations also strongly perturb cellularization, altering the timing and rate of furrow ingression. They cause dramatic vesiculation of new plasma membranes, and destabilize the stalk of cytoplasm that normally connects gastrulating cells to the yolk mass. A mutation closer to the N terminus blocks separation of pole cells with less effect on cellularization, highlighting mechanistic differences between contractile processes. Cumulatively, our data point to an important role for Anillin in scaffolding cleavage furrow components, directly stabilizing intracellular bridges, and indirectly stabilizing newly deposited plasma membrane during cellularization.