IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v415y2002i6868d10.1038_415192a.html
   My bibliography  Save this article

The motor domain determines the large step of myosin-V

Author

Listed:
  • Hiroto Tanaka

    (Single Molecule Processes Project, ICORP, JST)

  • Kazuaki Homma

    (University of Massachusetts Medical School)

  • Atsuko Hikikoshi Iwane

    (Graduate School of Medicine Osaka University)

  • Eisaku Katayama

    (Institute of Medical Science, The University of Tokyo
    PRESTO, Japan Science and Technology Corporation)

  • Reiko Ikebe

    (University of Massachusetts Medical School)

  • Junya Saito

    (University of Massachusetts Medical School)

  • Toshio Yanagida

    (Single Molecule Processes Project, ICORP, JST
    Graduate School of Medicine Osaka University)

  • Mitsuo Ikebe

    (University of Massachusetts Medical School)

Abstract

Class-V myosin proceeds along actin filaments with large (∼36 nm) steps1,2,3. Myosin-V has two heads, each of which consists of a motor domain and a long (23 nm) neck domain. In accordance with the widely accepted lever-arm model4, it was suggested that myosin-V steps to successive (36 nm) target zones along the actin helical repeat by tilting its long neck (lever-arm)5. To test this hypothesis, we measured the mechanical properties of single molecules of myosin-V truncation mutants with neck domains only one-sixth of the native length. Our results show that the processivity and step distance along actin are both similar to those of full-length myosin-V. Thus, the long neck domain is not essential for either the large steps or processivity of myosin-V. These results challenge the lever-arm model. We propose that the motor domain and/or the actomyosin interface enable myosin-V to produce large processive steps during translocation along actin.

Suggested Citation

  • Hiroto Tanaka & Kazuaki Homma & Atsuko Hikikoshi Iwane & Eisaku Katayama & Reiko Ikebe & Junya Saito & Toshio Yanagida & Mitsuo Ikebe, 2002. "The motor domain determines the large step of myosin-V," Nature, Nature, vol. 415(6868), pages 192-195, January.
    • Handle: RePEc:nat:nature:v:415:y:2002:i:6868:d:10.1038_415192a
    DOI: 10.1038/415192a
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/415192a
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/415192a?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.

    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:415:y:2002:i:6868:d:10.1038_415192a. 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.