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A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles

Nature volume 359, pages 543–547 (1992)Cite this article

Abstract

MITOSIS comprises a complex set of overlapping motile events, many of which involve microtubule-dependent motor enzymes1,2. Here we describe a new member of the kinesin superfamily. The protein was originally identified as a spindle antigen by the CHO1 monoclonal antibody3 and shown to be required for mitotic progression4,5. We have cloned the gene that encodes this antigen and found that its sequence contains a domain with strong sequence similarity to the motor domain of kinesin-like proteins. The product of this gene, expressed in bacteria, can cross-bridge antiparallel microtubules in vitro, and in the presence of Mg–ATP, microtubules slide over one another in a fashion reminiscent of microtubule movements during spindle elongation.

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Author notes

  1. Ryoko Kuriyama: Department of Cell Biology and Neuroanatomy, University of Minnesota, Minneapolis, Minnesota 55455, USA

Authors and Affiliations

  1. Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, 80309, USA

    Corey Nislow, Vivian A. Lombillo, Ryoko Kuriyama & J. Richard Mclntosh

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  1. Corey Nislow
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  2. Vivian A. Lombillo
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  3. Ryoko Kuriyama
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  4. J. Richard Mclntosh
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Nislow, C., Lombillo, V., Kuriyama, R. et al. A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles. Nature 359, 543–547 (1992). https://doi.org/10.1038/359543a0

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