IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v6y2015i1d10.1038_ncomms9730.html
   My bibliography  Save this article

Formin and capping protein together embrace the actin filament in a ménage à trois

Author

Listed:
  • Shashank Shekhar

    (Cytoskeleton Dynamics and Cell Motility, Biophysics and Structural Biology, I2BC, CNRS)

  • Mikael Kerleau

    (Cytoskeleton Dynamics and Cell Motility, Biophysics and Structural Biology, I2BC, CNRS
    Present address: Institut Jacques Monod, CNRS, Université Paris Diderot et Sorbonne Paris Cité, Paris, France.)

  • Sonja Kühn

    (Cytoskeleton Dynamics and Cell Motility, Biophysics and Structural Biology, I2BC, CNRS)

  • Julien Pernier

    (Cytoskeleton Dynamics and Cell Motility, Biophysics and Structural Biology, I2BC, CNRS)

  • Guillaume Romet-Lemonne

    (Cytoskeleton Dynamics and Cell Motility, Biophysics and Structural Biology, I2BC, CNRS
    Present address: Institut Jacques Monod, CNRS, Université Paris Diderot et Sorbonne Paris Cité, Paris, France.)

  • Antoine Jégou

    (Cytoskeleton Dynamics and Cell Motility, Biophysics and Structural Biology, I2BC, CNRS
    Present address: Institut Jacques Monod, CNRS, Université Paris Diderot et Sorbonne Paris Cité, Paris, France.)

  • Marie-France Carlier

    (Cytoskeleton Dynamics and Cell Motility, Biophysics and Structural Biology, I2BC, CNRS)

Abstract

Proteins targeting actin filament barbed ends play a pivotal role in motile processes. While formins enhance filament assembly, capping protein (CP) blocks polymerization. On their own, they both bind barbed ends with high affinity and very slow dissociation. Their barbed-end binding is thought to be mutually exclusive. CP has recently been shown to be present in filopodia and controls their morphology and dynamics. Here we explore how CP and formins may functionally coregulate filament barbed-end assembly. We show, using kinetic analysis of individual filaments by microfluidics-assisted fluorescence microscopy, that CP and mDia1 formin are able to simultaneously bind barbed ends. This is further confirmed using single-molecule imaging. Their mutually weakened binding enables rapid displacement of one by the other. We show that formin FMNL2 behaves similarly, thus suggesting that this is a general property of formins. Implications in filopodia regulation and barbed-end structural regulation are discussed.

Suggested Citation

  • Shashank Shekhar & Mikael Kerleau & Sonja Kühn & Julien Pernier & Guillaume Romet-Lemonne & Antoine Jégou & Marie-France Carlier, 2015. "Formin and capping protein together embrace the actin filament in a ménage à trois," Nature Communications, Nature, vol. 6(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9730
    DOI: 10.1038/ncomms9730
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms9730
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms9730?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
    ---><---

    Citations

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


    Cited by:

    1. Heidi Ulrichs & Ignas Gaska & Shashank Shekhar, 2023. "Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

    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:6:y:2015:i:1:d:10.1038_ncomms9730. 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.