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Minus-end-directed motion of kinesin–coated microspheres driven by microtubule depolymerization

Nature volume 373, pages 161–164 (1995)Cite this article

Abstract

DYNAMIC changes in microtubule (MT) length have long been thought to contribute to intracellular motility1. Both the polymerization2 and depolymerization3–5 of tubulin have been shown to do work in vitro, but the biochemical complexity of objects moved, such as chromosomes, has complicated the identifi-cation of proteins that couple MT dynamics with motility. Work with MTs grown from and tethered to pellicles of lysed Tetrahymena has shown that disassembly-dependent movement of chromo-somes in vitro can be inhibited with antibodies against the motor domain of kinesin6. To study proteins that can function in disassembly-dependent motion, we have refined this motility assay, replacing chromosomes with protein-coated latex microspheres. We report here the ability of several enzymes, including kinesin, to support in vitro motility of latex microspheres on disassembling MTs (Fig. la). The polarity of kinesin's motor activity can be reversed by MT disassembly and interactions between a motor and a MT end can either slow or speed the rate of tubulin depolymerization.

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Author notes

  1. Russell J. Stewart: Rowland Institute for Science, Cambridge, Massachusetts 02142, USA

  2. J. Richard McIntosh: To whom correspondence should be addressed.

Authors and Affiliations

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

    Vivian A. Lombillo, Russell J. Stewart & J. Richard McIntosh

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  1. Vivian A. Lombillo
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  2. Russell J. Stewart
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  3. J. Richard McIntosh
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Lombillo, V., Stewart, R. & Richard McIntosh, J. Minus-end-directed motion of kinesin–coated microspheres driven by microtubule depolymerization. Nature 373, 161–164 (1995). https://doi.org/10.1038/373161a0

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