IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v8y2017i1d10.1038_s41467-017-01745-4.html
   My bibliography  Save this article

mDia1 senses both force and torque during F-actin filament polymerization

Author

Listed:
  • Miao Yu

    (Mechanobiology Institute, National University of Singapore
    National University of Singapore)

  • Xin Yuan

    (Mechanobiology Institute, National University of Singapore)

  • Chen Lu

    (Mechanobiology Institute, National University of Singapore)

  • Shimin Le

    (Mechanobiology Institute, National University of Singapore
    National University of Singapore)

  • Ryo Kawamura

    (Mechanobiology Institute, National University of Singapore
    National University of Singapore)

  • Artem K. Efremov

    (Mechanobiology Institute, National University of Singapore)

  • Zhihai Zhao

    (Mechanobiology Institute, National University of Singapore
    National University of Singapore)

  • Michael M. Kozlov

    (Tel Aviv University)

  • Michael Sheetz

    (Mechanobiology Institute, National University of Singapore
    Columbia University)

  • Alexander Bershadsky

    (Mechanobiology Institute, National University of Singapore
    Weizmann Institute of Science)

  • Jie Yan

    (Mechanobiology Institute, National University of Singapore
    National University of Singapore
    National University of Singapore)

Abstract

Formins, an important family of force-bearing actin-polymerizing factors, function as homodimers that bind with the barbed end of actin filaments through a ring-like structure assembled from dimerized FH2 domains. It has been hypothesized that force applied to formin may facilitate transition of the FH2 ring from an inhibitory closed conformation to a permissive open conformation, speeding up actin polymerization. We confirm this hypothesis for mDia1 dependent actin polymerization by stretching a single-actin filament in the absence of profilin using magnetic tweezers, and observe that increasing force from 0.5 to 10 pN can drastically speed up the actin polymerization rate. Further, we find that this force-promoted actin polymerization requires torsionally unconstrained actin filament, suggesting that mDia1 also senses torque. As actin filaments are subject to complex mechanical constraints in living cells, these results provide important insights into how formin senses these mechanical constraints and regulates actin organization accordingly.

Suggested Citation

  • Miao Yu & Xin Yuan & Chen Lu & Shimin Le & Ryo Kawamura & Artem K. Efremov & Zhihai Zhao & Michael M. Kozlov & Michael Sheetz & Alexander Bershadsky & Jie Yan, 2017. "mDia1 senses both force and torque during F-actin filament polymerization," Nature Communications, Nature, vol. 8(1), pages 1-9, December.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01745-4
    DOI: 10.1038/s41467-017-01745-4
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-017-01745-4
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-017-01745-4?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. Yee Han Tee & Wei Jia Goh & Xianbin Yong & Hui Ting Ong & Jinrong Hu & Ignacius Yan Yun Tay & Shidong Shi & Salma Jalal & Samuel F. H. Barnett & Pakorn Kanchanawong & Wenmao Huang & Jie Yan & Yong Ann, 2023. "Actin polymerisation and crosslinking drive left-right asymmetry in single cell and cell collectives," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Sayaka Sekine & Mitsusuke Tarama & Housei Wada & Mustafa M. Sami & Tatsuo Shibata & Shigeo Hayashi, 2024. "Emergence of periodic circumferential actin cables from the anisotropic fusion of actin nanoclusters during tubulogenesis," Nature Communications, Nature, vol. 15(1), pages 1-13, 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:8:y:2017:i:1:d:10.1038_s41467-017-01745-4. 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.