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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.

Original publication

DOI

10.1093/emboj/19.21.5711

Type

Journal article

Journal

EMBO J

Publication Date

01/11/2000

Volume

19

Pages

5711 - 5719

Keywords

Base Sequence, Cell Division, DNA Primers, HeLa Cells, Humans, Kinesin, Microscopy, Fluorescence, Recombinant Proteins, Transfection, Two-Hybrid System Techniques, rab GTP-Binding Proteins