Division of Translational Medicine, Wadsworth Center, NYS Department of Health, Empire State Plaza, PO Box 509, Albany, NY 12201-0509, USA.
Cell Mol Life Sci. 2013 Apr;70(7):1285-96. doi: 10.1007/s00018-012-1205-0. Epub 2012 Nov 17.
The M-type kinesin isoform, Kif9, has recently been implicated in maintaining a physical connection between the centrosome and nucleus in Dictyostelium discoideum. However, the mechanism by which Kif9 functions to link these two organelles remains obscure. Here we demonstrate that the Kif9 protein is localized to the nuclear envelope and is concentrated in the region underlying the centrosome point of attachment. Nuclear anchorage appears mediated through a specialized transmembrane domain located in the carboxyl terminus. Kif9 interacts with microtubules in in vitro binding assays and effects an endwise depolymerization of the polymer. These results suggest a model whereby Kif9 is anchored to the nucleus and generates a pulling force that reels the centrosome up against the nucleus. This is a novel activity for a kinesin motor, one important for progression of cells into mitosis and to ensure centrosome-nuclear parity in a multinuclear environment.
M 型驱动蛋白同工型 Kif9 最近被牵涉到在粘菌盘基网柄菌中维持着中心体和核之间的物理连接。然而,Kif9 发挥连接这两个细胞器的功能的机制仍然不清楚。在这里,我们证明 Kif9 蛋白定位于核膜上,并集中在中心体附着点的下方区域。核锚定似乎通过位于羧基末端的特殊跨膜结构域介导。Kif9 在体外结合测定中与微管相互作用,并对聚合物进行末端解聚。这些结果表明了一种模型,即 Kif9 锚定在核上,并产生拉力,将中心体拉向核。这是驱动蛋白马达的一种新活性,对于细胞进入有丝分裂以及确保多核环境中的中心体-核均等性非常重要。