Local change in phospholipid composition at the cleavage furrow is essential for completion of cytokinesis
Local change in phospholipid composition at the cleavage furrow is essential for completion of cytokinesis
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DOI：
10.1074/jbc.m504282200
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发表时间：
2005-11-11
影响因子：
4.8
通讯作者：
Umeda, M
中科院分区：
文献类型：
--
作者：
Emoto, K;Inadome, H;Umeda, M
细胞分裂最终导致两个子细胞的膜分离，大概是通过膜融合，需要膜脂的分布和组成的动态变化。我们之前已经证明，在胞质分裂后期，膜脂磷脂酰乙醇胺（PE）暴露在卵裂沟的细胞表面，并且这种PE运动参与了收缩环解体的调节。在这里，我们表明，PE 结合肽对细胞表面 PE 的固定可阻止胞质分裂后期 RhoA 失活。磷脂酰肌醇 4-磷酸 5-激酶 (PIP5K)，但不是其他 RhoA 效应子，与肽处理的细胞中的 RhoA 共定位。事实上，PIP5K 及其产物磷脂酰肌醇 4,5-二磷酸 (PI(4,5) P-2) 定位于正常分裂细胞的卵裂沟。激酶缺陷型 PIP5K 突变体的过度表达和抗 PI(4,5) P-2 抗体的显微注射均通过阻止 PI(4,5) P-2 在卵裂沟中的局部积累来损害胞质分裂。这些发现表明，PI(4,5) P-2 的局部产生对于胞质分裂的正确完成是必需的，并且在卵裂沟膜中可能形成独特的脂质结构域可能在胞质分裂后期协调收缩重排与膜重塑中发挥关键作用。
Cell division ends up with the membrane separation of two daughter cells, presumably by a membrane fusion that requires dynamic changes of the distribution and the composition of membrane lipids. We have previously shown that a membrane lipid phosphatidylethanolamine ( PE) is exposed on the cell surface of the cleavage furrow during late cytokinesis and that this PE movement is involved in regulation of the contractile ring disassembly. Here we show that immobilization of cell surface PE by a PE-binding peptide blocks the RhoA inactivation in the late stage of cytokinesis. Phosphatidylinositol 4-phosphate5-kinase (PIP5K), but not other RhoA effectors, is co-localized with RhoA in the peptide-treated cells. Indeed, PIP5K and its product phosphatidylinositol 4,5-bisphosphate (PI(4,5) P-2) are localized to the cleavage furrow of normally dividing cells. Both overexpression of a kinase-deficient PIP5K mutant and microinjection of anti-PI(4,5) P-2 antibodies compromise cytokinesis by preventing local accumulation of PI(4,5) P-2 in the cleavage furrow. These findings demonstrate that the localized production of PI(4,5) P-2 is required for the proper completion of cytokinesis and that the possible formation of a unique lipid domain in the cleavage furrow membrane may play a crucial role in coordinating the contractile rearrangement with the membrane remodeling during late cytokinesis.