IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v10y2019i1d10.1038_s41467-019-13160-y.html
   My bibliography  Save this article

Myosin 1b is an actin depolymerase

Author

Listed:
  • Julien Pernier

    (PSL Research University, CNRS UMR168
    Sorbonne Université
    Institut Curie, PSL Research University and C.N.R.S. UMR 144)

  • Remy Kusters

    (PSL Research University, CNRS UMR168
    Sorbonne Université
    Center for Research and Interdisciplinarity (CRI))

  • Hugo Bousquet

    (Sorbonne Université
    Institut Curie, PSL Research University and C.N.R.S. UMR 144)

  • Thibaut Lagny

    (PSL Research University, CNRS UMR168
    Sorbonne Université
    Institut Curie, PSL Research University and C.N.R.S. UMR 144)

  • Antoine Morchain

    (PSL Research University, CNRS UMR168
    Sorbonne Université)

  • Jean-François Joanny

    (PSL Research University, CNRS UMR168
    Sorbonne Université
    ESPCI Paris, PSL Research University
    Collège de France)

  • Patricia Bassereau

    (PSL Research University, CNRS UMR168
    Sorbonne Université)

  • Evelyne Coudrier

    (Sorbonne Université
    Institut Curie, PSL Research University and C.N.R.S. UMR 144)

Abstract

The regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here we investigate the contribution of myosin 1b to actin dynamics using sliding motility assays. We observe that sliding on myosin 1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as another type of depolymerase and points to its singular interactions with the actin barbed end.

Suggested Citation

  • Julien Pernier & Remy Kusters & Hugo Bousquet & Thibaut Lagny & Antoine Morchain & Jean-François Joanny & Patricia Bassereau & Evelyne Coudrier, 2019. "Myosin 1b is an actin depolymerase," Nature Communications, Nature, vol. 10(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13160-y
    DOI: 10.1038/s41467-019-13160-y
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-019-13160-y
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-019-13160-y?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
    ---><---

    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:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13160-y. 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.