Loading direction regulates the affinity of ADP for kinesin

Sotaro Uemura, Shin'ichi Ishiwata

    Research output: Contribution to journalArticle

    97 Citations (Scopus)

    Abstract

    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
    Volume10
    Issue number4
    DOIs
    Publication statusPublished - 2003 Apr 1

    Fingerprint

    Kinesin
    Adenosine Diphosphate
    Microtubules
    Adenosine Triphosphatases
    Head
    Adenosine Triphosphate
    Molecules
    Direction compound

    ASJC Scopus subject areas

    • Biochemistry
    • Structural Biology
    • Genetics

    Cite this

    Loading direction regulates the affinity of ADP for kinesin. / Uemura, Sotaro; Ishiwata, Shin'ichi.

    In: Nature Structural Biology, Vol. 10, No. 4, 01.04.2003, p. 308-311.

    Research output: Contribution to journalArticle

    Uemura, Sotaro ; Ishiwata, Shin'ichi. / Loading direction regulates the affinity of ADP for kinesin. In: Nature Structural Biology. 2003 ; Vol. 10, No. 4. pp. 308-311.
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