IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v411y2001i6836d10.1038_35078000.html
   My bibliography  Save this article

Switch-based mechanism of kinesin motors

Author

Listed:
  • Masahide Kikkawa

    (Graduate School of Medicine, University of Tokyo)

  • Elena P. Sablin

    (University of California)

  • Yasushi Okada

    (Graduate School of Medicine, University of Tokyo)

  • Hiroaki Yajima

    (Graduate School of Medicine, University of Tokyo)

  • Robert J. Fletterick

    (University of California)

  • Nobutaka Hirokawa

    (Graduate School of Medicine, University of Tokyo)

Abstract

Kinesin motors are specialized enzymes that use hydrolysis of ATP to generate force and movement along their cellular tracks, the microtubules. Although numerous biochemical and biophysical studies have accumulated much data that link microtubule-assisted ATP hydrolysis to kinesin motion, the structural view of kinesin movement remains unclear. This study of the monomeric kinesin motor KIF1A combines X-ray crystallography and cryo-electron microscopy, and allows analysis of force-generating conformational changes at atomic resolution. The motor is revealed in its two functionally critical states—complexed with ADP and with a non-hydrolysable analogue of ATP. The conformational change observed between the ADP-bound and the ATP-like structures of the KIF1A catalytic core is modular, extends to all kinesins and is similar to the conformational change used by myosin motors and G proteins. Docking of the ADP-bound and ATP-like crystallographic models of KIF1A into the corresponding cryo-electron microscopy maps suggests a rationale for the plus-end directional bias associated with the kinesin catalytic core.

Suggested Citation

  • Masahide Kikkawa & Elena P. Sablin & Yasushi Okada & Hiroaki Yajima & Robert J. Fletterick & Nobutaka Hirokawa, 2001. "Switch-based mechanism of kinesin motors," Nature, Nature, vol. 411(6836), pages 439-445, May.
    • Handle: RePEc:nat:nature:v:411:y:2001:i:6836:d:10.1038_35078000
    DOI: 10.1038/35078000
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35078000
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35078000?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Matthieu P. M. H. Benoit & Lu Rao & Ana B. Asenjo & Arne Gennerich & Hernando Sosa, 2024. "Cryo-EM unveils kinesin KIF1A’s processivity mechanism and the impact of its pathogenic variant P305L," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Byron Hunter & Matthieu P. M. H. Benoit & Ana B. Asenjo & Caitlin Doubleday & Daria Trofimova & Corey Frazer & Irsa Shoukat & Hernando Sosa & John S. Allingham, 2022. "Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    3. Ray, Krishanu, 2006. "How kinesins walk, assemble and transport: A birds-eye-view of some unresolved questions," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 372(1), pages 52-64.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:411:y:2001:i:6836:d:10.1038_35078000. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.