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First published online 6 January 2004
doi: 10.1242/jcs.00892

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A role for the spectrin superfamily member Syne-1 and kinesin II in cytokinesis

Department of Cell Biology and Human Anatomy, School of Medicine, University of California, Davis, CA 95616, USA

^* Author for correspondence (e-mail: kabeck{at}ucdavis.edu)

Accepted 18 September 2003

Expression of a dominant negative fragment of the spectrin family member Syne-1 causes an accumulation of binucleate cells, suggesting a role for this protein in cytokinesis. An association of this fragment with the C-terminal tail domain of the kinesin II subunit KIF3B was identified by yeast two-hybrid and co-precipitation assays, suggesting that the role of Syne-1 in cytokinesis involves an interaction with kinesin II. In support of this we found that (1) expression of KIF3B tail domain also gives rise to multinucleate cells, (2) both Syne-1 and KIF3B localize to the central spindle and midbody during cytokinesis in a detergent resistant and ATP sensitive manner and (3) Syne-1 localization is blocked by expression of KIF3B tail. Also, membrane vesicles containing syntaxin associate with the spindle midbody with identical properties. We conclude that Syne-1 and KIF3B function together in cytokinesis by facilitating the accumulation of membrane vesicles at the spindle midbody.

Key words: Kinesin, Cytokinesis, Mitosis, Golgi, Spectrin, Vesicle transport

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