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• W2791508075 abstract "Kinesin-1 is a nanoscale molecular motor that walks towards the fast-growing (plus) ends of microtubules, hauling molecular cargo to specific reaction sites in cells. Kinesin-driven transport is central to the self-organization of eukaryotic cells and shows great promise as a tool for nano-engineering 1 . Recent work hints that kinesin may also play a role in modulating the stability of its microtubule track, both in vitro2,3 and in vivo 4 , but the results are conflicting5–7 and the mechanisms are unclear. Here, we report a new dimension to the kinesin–microtubule interaction, whereby strong-binding state (adenosine triphosphate (ATP)-bound and apo) kinesin-1 motor domains inhibit the shrinkage of guanosine diphosphate (GDP) microtubules by up to two orders of magnitude and expand their lattice spacing by ~1.6%. Our data reveal an unexpected mechanism by which the mechanochemical cycles of kinesin and tubulin interlock, and so allow motile kinesins to influence the structure, stability and mechanics of their microtubule track. Kinesins, natural nanometre-scale stepper motors, can feed back on the structure and dynamics of their microtubule tracks." @default.
• W2791508075 created "2018-03-29" @default.
• W2791508075 creator A5053899256 @default.
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• W2791508075 date "2018-03-12" @default.
• W2791508075 modified "2023-10-04" @default.
• W2791508075 title "Kinesin expands and stabilizes the GDP-microtubule lattice" @default.
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• W2791508075 doi "https://doi.org/10.1038/s41565-018-0084-4" @default.
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