Kinesin-microtubule binding depends on both nucleotide state and loading direction

Sotaro Uemura, Kenji Kawaguchi, Junichiro Yajima, Masaki Edamatsu, Yoko Yano Toyoshima, Shin'ichi Ishiwata*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    107 Citations (Scopus)


    Kinesin is a motor protein that transports organelles along a microtubule toward its plus end by using the energy of ATP hydrolysis. To clarify the nucleotide-dependent binding mode, we measured the unbinding force for one-headed kinesin heterodimers in addition to conventional two-headed kinesin homodimers under several nucleotide states. We found that both a weak and a strong binding state exist in each head of kinesin corresponding to a small and a large unbinding force, respectively; that is, weak for the ADP state and strong for the nucleotide-free and adenosine 5′-[β,γ-imido]triphosphate states. Model analysis showed that (i) the two binding modes in each head could be explained by a difference in the binding energy and (ii) the directional instability of binding, i.e., dependence of unbinding force on loading direction, could be explained by a difference in the characteristic distance for the kinesin-microtubule interaction during plus- and minus-end-directed loading. Both these factors must play an important role in the molecular mechanism of kinesin motility.

    Original languageEnglish
    Pages (from-to)5977-5981
    Number of pages5
    JournalProceedings of the National Academy of Sciences of the United States of America
    Issue number9
    Publication statusPublished - 2002 Apr 30

    ASJC Scopus subject areas

    • Genetics
    • General


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