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| The EMBO Journal
(2000) 19, 5711–5719, doi:10.1093/emboj/19.21.5711 |
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| The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis |
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| Elaine Hill1, Mairi Clarke1 and Francis A. Barr1, 2 |
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1 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 2 Max Planck Institute for Biochemistry, Department of Cell Biology, Am Klopferspitz 18a, Martinsried, D-82152, Germany To whom correspondence should be addressed Francis A. Barr, barr@biochem.mpg.de Received 26 June 2000; Revised 8 September 2000; Accepted 8 September 2000. |
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| Abstract |
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| 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. |
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| Keywords: cytokinesis, Golgi, kinesin, mitosis, Rab |
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