In vitro contraction of cytokinetic ring depends on myosin II but not on actin dynamics
In vitro contraction of cytokinetic ring depends on myosin II but not on actin dynamics
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DOI：
10.1038/ncb2781
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发表时间：
2013-07-01
影响因子：
21.3
通讯作者：
Mabuchi, Issei
中科院分区：
文献类型：
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作者：
Mishra, Mithilesh;Kashiwazaki, Jun;Mabuchi, Issei
许多真核生物中的细胞分裂涉及基于肌动球蛋白的收缩环的收缩(1,2)。然而，收缩环收缩的详细机制尚不完全清楚。在这里，我们建立了一个实验系统来研究环在体外完成收缩。我们发现，在没有其他细胞质成分的情况下，透化裂殖酵母细胞的收缩环以 ATP 和肌球蛋白 II 依赖性方式经历快速收缩。令人惊讶的是，尽管添加外源肌动蛋白交联蛋白会阻止环收缩，但肌动蛋白聚合及其分解都不是收缩环收缩所必需的。使用裂殖酵母胞质分裂突变体产生的收缩环，我们表明并非环组装所需的所有蛋白质都是其体外收缩所必需的。我们的工作为最小的具有收缩能力的细胞因子环装置的定义提供了开始。
Cytokinesis in many eukaryotes involves the contraction of an actomyosin-based contractile ring(1,2). However, the detailed mechanism of contractile ring contraction is not fully understood. Here, we establish an experimental system to study contraction of the ring to completion in vitro. We show that the contractile ring of permeabilized fission yeast cells undergoes rapid contraction in an ATP- and myosin-II-dependent manner in the absence of other cytoplasmic constituents. Surprisingly, neither actin polymerization nor its disassembly is required for contraction of the contractile ring, although addition of exogenous actin-crosslinking proteins blocks ring contraction. Using contractile rings generated from fission yeast cytokinesis mutants, we show that not all proteins required for assembly of the ring are required for its contraction in vitro. Our work provides the beginnings of the definition of a minimal contraction-competent cytokinetic ring apparatus.