Department of Molecular Cellular and Developmental Biology, Yale University, PO Box 208103, New Haven, CT 06520-8103, USA.
Department of Molecular Cellular and Developmental Biology, Yale University, PO Box 208103, New Haven, CT 06520-8103, USA Department of Molecular Biophysics and Biochemistry, Yale University, PO Box 208103, New Haven, CT 06520-8103, USA Department of Cell Biology, Yale University, PO Box 208103, New Haven, CT 06520-8103, USA
J Cell Sci. 2015 Jul 1;128(13):2259-68. doi: 10.1242/jcs.162974. Epub 2015 May 14.
F-BAR proteins are known to participate in cytokinesis, but their mechanisms are not well understood. Here we investigated Rga7p, an Schizosaccharomyces pombe F-BAR protein with a RhoGAP domain. Localization of Rga7p to the cytokinetic cleavage furrow depends on its F-BAR domain, actin filaments, the formins Cdc12p and For3p, and the presence of a contractile ring. Rga7p is not required for the constriction of the contractile ring but does participate in the transport of a β-glucan synthetase (Bgs4p) from the late Golgi compartments to plasma membrane that is adjacent to the contractile ring. Cells without Rga7p moved Bgs4p normally from the poles to the Golgi complex near to the cell center, but Bgs4p then moved slowly from the late Golgi compartments to the cleavage site. The late arrival and lower than normal numbers of Bgs4p result in septal defects late in cytokinesis, and in the lysis of separating cells, similar to that in cells with mutations in the cwg1(+) gene (which encodes Bgs4p).
F-BAR 蛋白已知参与胞质分裂,但它们的机制尚不清楚。在这里,我们研究了 Schizosaccharomyces pombe 的 F-BAR 蛋白 Rga7p,它具有 RhoGAP 结构域。Rga7p 在有丝分裂分裂沟的定位取决于其 F-BAR 结构域、肌动蛋白丝、formin 蛋白 Cdc12p 和 For3p,以及收缩环的存在。Rga7p 不是收缩环收缩所必需的,但确实参与了将 β-葡聚糖合成酶(Bgs4p)从晚期高尔基体区室运送到与收缩环相邻的质膜。没有 Rga7p 的细胞可以正常地将 Bgs4p 从两极运送到靠近细胞中心的高尔基体复合体,但随后 Bgs4p 从晚期高尔基体区室缓慢地移动到分裂位点。Bgs4p 的迟来和数量低于正常水平导致胞质分裂后期出现隔膜缺陷,并导致正在分离的细胞裂解,类似于 cwg1(+)基因(编码 Bgs4p)突变细胞的情况。