Abstract
The mammalian genome possesses 45 unique genes that code for kinesins. Kinesins are motor molecules, ATPases, which are specialized for the transport of cellular materials along the surface of cellular microtubules. Microtubules consist of linear polymers of repeating 8-nm-long tubulin dimers, each of which comprises one binding site for the kinesin motor domain. Kinesins “walk” from one binding site to the next, hydrolyzing one ATP with every step. In addition to their transport roles, these enzymes also remodel microtubules, engineer mitotic spindle assembly, and assist with chromosome segregation in dividing cells. Thus far, kinesins have been identified to operate in every conceivable microtubule-based process in the cell. Their diversity has enabled researchers to study disparate microtubule-based processes in isolation by selective disruption of individual kinesin motors. Functional characterization of microtubule-dependent activities with such high precision would not be possible using microtubule drugs, most of which globally disrupt all microtubule processes simultaneously. For this reason, kinesins have recently become attractive targets for the development of chemotherapeutic drugs.
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Acknowledgments
I am indebted to Mike Wagenbach for preparing Fig. 3.1a. The research in Linda Wordeman’s laboratory is supported by the National Institutes of Health (GM069429) and the National Science Foundation (MCB-1041173).
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Wordeman, L. (2012). The Kinesin Superfamily. In: Kavallaris, M. (eds) Cytoskeleton and Human Disease. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-788-0_3
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