IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v10y2019i1d10.1038_s41467-019-10964-w.html
   My bibliography  Save this article

Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion

Author

Listed:
  • N. O. Alieva

    (National University of Singapore, T-lab)

  • A. K. Efremov

    (National University of Singapore, T-lab
    National University of Singapore)

  • S. Hu

    (National University of Singapore, T-lab)

  • D. Oh

    (National University of Singapore, T-lab)

  • Z. Chen

    (National University of Singapore, T-lab
    University of California)

  • M. Natarajan

    (National University of Singapore, T-lab)

  • H. T. Ong

    (National University of Singapore, T-lab)

  • A. Jégou

    (Institut Jacques Monod, CNRS, Université de Paris)

  • G. Romet-Lemonne

    (Institut Jacques Monod, CNRS, Université de Paris)

  • J. T. Groves

    (National University of Singapore, T-lab
    University of California)

  • M. P. Sheetz

    (National University of Singapore, T-lab
    Columbia University)

  • J. Yan

    (National University of Singapore, T-lab
    National University of Singapore
    National University of Singapore)

  • A. D. Bershadsky

    (National University of Singapore, T-lab
    Weizmann Institute of Science)

Abstract

Filopodia, dynamic membrane protrusions driven by polymerization of an actin filament core, can adhere to the extracellular matrix and experience both external and cell-generated pulling forces. The role of such forces in filopodia adhesion is however insufficiently understood. Here, we study filopodia induced by overexpression of myosin X, typical for cancer cells. The lifetime of such filopodia positively correlates with the presence of myosin IIA filaments at the filopodia bases. Application of pulling forces to the filopodia tips through attached fibronectin-coated laser-trapped beads results in sustained growth of the filopodia. Pharmacological inhibition or knockdown of myosin IIA abolishes the filopodia adhesion to the beads. Formin inhibitor SMIFH2, which causes detachment of actin filaments from formin molecules, produces similar effect. Thus, centripetal force generated by myosin IIA filaments at the base of filopodium and transmitted to the tip through actin core in a formin-dependent fashion is required for filopodia adhesion.

Suggested Citation

  • N. O. Alieva & A. K. Efremov & S. Hu & D. Oh & Z. Chen & M. Natarajan & H. T. Ong & A. Jégou & G. Romet-Lemonne & J. T. Groves & M. P. Sheetz & J. Yan & A. D. Bershadsky, 2019. "Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10964-w
    DOI: 10.1038/s41467-019-10964-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-019-10964-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-019-10964-w?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. Ze Gong & Koen Dries & Rodrigo A. Migueles-Ramírez & Paul W. Wiseman & Alessandra Cambi & Vivek B. Shenoy, 2023. "Chemo-mechanical diffusion waves explain collective dynamics of immune cell podosomes," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Guilherme Ventura & Aboutaleb Amiri & Raghavan Thiagarajan & Mari Tolonen & Amin Doostmohammadi & Jakub Sedzinski, 2022. "Multiciliated cells use filopodia to probe tissue mechanics during epithelial integration in vivo," Nature Communications, Nature, vol. 13(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:10:y:2019:i:1:d:10.1038_s41467-019-10964-w. 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.