Article
- The EMBO Journal (2000) 19, 5711 - 5719
- doi:10.1093/emboj/19.21.5711
The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis
Elaine Hill1, Mairi Clarke1 and Francis A. Barr1,2
- 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
- Max Planck Institute for Biochemistry, Department of Cell Biology, Am Klopferspitz 18a, Martinsried, D-82152, Germany
Correspondence to:
Francis A. Barr, E-mail: barr@biochem.mpg.de
Received 26 June 2000; Accepted 8 September 2000; Revised 8 September 2000
Abstract
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.
Keywords:
- cytokinesis,
- Golgi,
- kinesin,
- mitosis,
- Rab
