Arasada Rajesh, Pollard Thomas D
Department of Molecular Cellular and Developmental Biology, Yale University, P.O. Box 208103, New Haven, CT 06520-8103 USA.
Department of Molecular Cellular and Developmental Biology, Yale University, P.O. Box 208103, New Haven, CT 06520-8103 USA; Department of Molecular Biophysics and Biochemistry, Yale University, P.O. Box 208103, New Haven, CT 06520-8103 USA; Department of Cell Biology, Yale University, P.O. Box 208103, New Haven, CT 06520-8103 USA.
Cell Rep. 2014 Sep 11;8(5):1533-44. doi: 10.1016/j.celrep.2014.07.048. Epub 2014 Aug 21.
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 ∼ 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.
已知Cdc15p在裂殖酵母的胞质分裂中发挥作用；然而，组装肌动蛋白和肌球蛋白的收缩环并不需要该蛋白，但它有助于将收缩环锚定在质膜上。Cdc15p具有一个脂质结合F - BAR结构域，这表明它在质膜和收缩环蛋白之间提供了物理连接。然而，我们发现Cdc15p在胞质分裂过程中更重要的功能是帮助将一种跨膜酶Bgs1p（也称为Cps1p）从高尔基体运输到质膜，在那里它似乎锚定了收缩环。Bgs1p在分裂沟中合成细胞壁，但其酶活性对于锚定收缩环并非必需。我们估计大约需要2000个Bgs1p分子来锚定收缩环。没有Bgs1p锚定，收缩环会沿着质膜滑动，这种现象依赖于一种名为Myp2p的非常规II型肌球蛋白。
