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A more recent version of this article appeared on February 1, 2006
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Submitted on June 17, 2005
Revised on November 28, 2005
Accepted on November 29, 2005
*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;
Martin-Luther-Universität Halle-Wittenberg, Biozentrum, D-06099 Halle, Germany
Monitoring Editor: J. Richard McIntosh
Conventional kinesin is an 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, while 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 YFP 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.
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