Hill E, Clarke M, Barr F A
Beatson Institute for Cancer Research, and University of Glasgow Institute of Biological and Life Sciences, CRC-Beatson Laboratories, Garscube Estate, Switchback Road, Bearsden, Glasgow G61 1BD, UK.
EMBO J. 2000 Nov 1;19(21):5711-9. doi: 10.1093/emboj/19.21.5711.
The Rab6-binding kinesin, Rab6-KIFL, was identified in a two-hybrid screen for proteins that interact with Rab6, a small GTPase involved in membrane traffic through the Golgi apparatus. We find that Rab6-KIFL accumulates in mitotic cells where it localizes to the midzone of the spindle during anaphase, and to the cleavage furrow and midbody during telophase. Overexpression of Rab6-KIFL causes a cell division defect resulting in cell death. Microinjection of antibodies to Rab6-KIFL results in the cells becoming binucleate after one cell cycle, and time-lapse microscopy reveals that this is due to a defect in cleavage furrow formation and thus cytokinesis. These data show that endogenous Rab6-KIFL functions in cell division during cleavage furrow formation and cytokinesis, in addition to its previously described role in membrane traffic.
在一项针对与Rab6相互作用的蛋白质的双杂交筛选中，鉴定出了与Rab6结合的驱动蛋白Rab6-KIFL。Rab6是一种参与通过高尔基体的膜运输的小GTP酶。我们发现Rab6-KIFL在有丝分裂细胞中积累，在后期定位于纺锤体的中区，在末期定位于分裂沟和中间体。Rab6-KIFL的过表达导致细胞分裂缺陷，进而导致细胞死亡。显微注射针对Rab6-KIFL的抗体，会使细胞在一个细胞周期后变成双核，延时显微镜显示这是由于分裂沟形成缺陷，从而导致胞质分裂出现问题。这些数据表明，内源性Rab6-KIFL除了在膜运输中发挥其先前描述的作用外，还在分裂沟形成和胞质分裂过程中的细胞分裂中发挥作用。
