Loading direction regulates the affinity of ADP for kinesin

Sotaro Uemura, Shin'ichi Ishiwata*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    104 Citations (Scopus)


    Kinesin is an ATP-driven molecular motor that moves processively along a microtubule. Processivity has been explained as a mechanism that involves alternating single- and double-headed binding of kinesin to microtubules coupled to the ATPase cycle of the motor. The internal load imposed between the two bound heads has been proposed to be a key factor regulating the ATPase cycle in each head. Here we show that external load imposed along the direction of motility on a single kinesin molecule enhances the binding affinity of ADP for kinesin, whereas an external load imposed against the direction of motility decreases it. This coupling between loading direction and enzymatic activity is in accord with the idea that the internal load plays a key role in the unidirectional and cooperative movement of processive motors.

    Original languageEnglish
    Pages (from-to)308-311
    Number of pages4
    JournalNature Structural Biology
    Issue number4
    Publication statusPublished - 2003 Apr 1

    ASJC Scopus subject areas

    • Biochemistry
    • Structural Biology
    • Genetics


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