Contractile Ring Stability in S-pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex
Contractile Ring Stability in S-pombe Depends on F-BAR Protein Cdc15p and Bgs1p Transport from the Golgi Complex
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DOI：
10.1016/j.celrep.2014.07.048
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发表时间：
2014-09-11
期刊：
影响因子：
8.8
通讯作者：
Pollard, Thomas D.
中科院分区：
文献类型：
--
作者：
Arasada, Rajesh;Pollard, Thomas D.
已知cdc 15 p有助于分裂酵母的胞质分裂;然而，该蛋白质并不需要组装肌动蛋白和肌球蛋白的收缩环，但它有助于将环锚在质膜上。Cdc 15 p具有脂质结合的F-BAR结构域，这表明它提供了质膜和收缩环蛋白之间的物理联系。然而，我们发现，胞质分裂过程中Cdc 15 p的一个更重要的功能是帮助提供一种跨膜酶，Bgs 1 p（也称为Cps 1 p），从高尔基体的质膜，在那里它似乎锚的收缩环。bgs 1 p在卵裂沟中合成细胞壁，但它的酶活性不需要锚收缩环。我们估计需要大约2，000个Bgs 1 p分子来锚环。没有Bgs 1 p锚，收缩环沿着质膜滑动，这种现象取决于一种称为Myp 2 p的非传统II型肌球蛋白。
Cdc15p is known to contribute to cytokinesis in fission yeast; however, the protein is not required to assemble the contractile ring of actin and myosin, but it helps to anchor the ring to the plasma membrane. Cdc15p has a lipid-binding F-BAR domain, suggesting that it provides a physical link between the plasma membrane and contractile ring proteins. However, we find that a more important function of Cdc15p during cytokinesis is to help deliver a transmembrane enzyme, Bgs1p (also called Cps1p), from the Golgi apparatus to the plasma membrane, where it appears to anchor the contractile ring. Bgs1p synthesizes the cell wall in the cleavage furrow, but its enzyme activity is not required to anchor the contractile ring. We estimate that similar to 2,000 Bgs1p molecules are required to anchor the ring. Without Bgs1p anchors, contractile rings slide along the plasma membrane, a phenomenon that depends on an unconventional type II myosin called Myp2p.