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Vol. 17, Issue 2, 907-916, February 2006

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Conventional Kinesin Mediates Microtubule-Microtubule Interactions In Vivo

Anne Straube ^* , Gerd Hause , Gero Fink ^*, and Gero Steinberg ^*

^* Max-Planck-Institut für terrestrische Mikrobiologie, D-35043 Marburg, Germany; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland, United Kingdom; and Martin-Luther-Universität Halle-Wittenberg, Biozentrum, D-06099 Halle, Germany

Submitted June 17, 2005; Revised November 28, 2005; Accepted November 29, 2005
Monitoring Editor: J. Richard McIntosh

Conventional kinesin is a ubiquitous organelle transporter that moves cargo toward the plus-ends of microtubules. In addition, several in vitro studies indicated a role of conventional kinesin in cross-bridging and sliding microtubules, but in vivo evidence for such a role is missing. In this study, we show that conventional kinesin mediates microtubule-microtubule interactions in the model fungus Ustilago maydis. Live cell imaging and ultrastructural analysis of various mutants in Kin1 revealed that this kinesin-1 motor is required for efficient microtubule bundling and participates in microtubule bending in vivo. High levels of Kin1 led to increased microtubule bending, whereas a rigor-mutation in the motor head suppressed all microtubule motility and promoted strong microtubule bundling, indicating that kinesin can form cross-bridges between microtubules in living cells. This effect required a conserved region in the C terminus of Kin1, which was shown to bind microtubules in vitro. In addition, a fusion protein of yellow fluorescent protein and the Kin1tail localized to microtubule bundles, further supporting the idea that a conserved microtubule binding activity in the tail of conventional kinesins mediates microtubule-microtubule interactions in vivo.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Gero Steinberg (gero.steinberg{at}staff.uni-marburg.de).

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