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    New insights into the mechanism of force generation by Kinesin-5 molecular motors

    Goulet, Adeline and Moores, Carolyn A. (2013) New insights into the mechanism of force generation by Kinesin-5 molecular motors. In: Jeon, K.W. (ed.) International Review of Cell and Molecular Biology. New York, U.S.: Elsevier, pp. 419-466. ISBN 9780124076969.

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    Kinesin-5 motors are members of a superfamily of microtubule-dependent ATPases and are widely conserved among eukaryotes. Kinesin-5s typically form homotetramers with pairs of motor domains located at either end of a dumbbell-shaped molecule. This quaternary structure enables cross-linking and ATP-driven sliding of pairs of microtubules, although the exact molecular mechanism of this activity is still unclear. Kinesin-5 function has been characterized in greatest detail in cell division, although a number of interphase roles have also been defined. The kinesin-5 ATPase is tuned for slow microtubule sliding rather than cellular transport and—in vertebrates—can be inhibited specifically by allosteric small molecules currently in cancer clinical trials. The biophysical and structural basis of kinesin-5 mechanochemistry is being elucidated and has provided further insight into kinesin-5 activities. However, it is likely that the precise mechanism of these important motors has evolved according to functional context and regulation in individual organisms.


    Item Type: Book Section
    Keyword(s) / Subject(s): ATPase, Force generation, Kinesin, Microtubule, Mitosis, Motor, Monastrol, Spindle
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 27 Jun 2013 10:24
    Last Modified: 02 Aug 2023 17:06


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