IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v466y2010i7303d10.1038_nature09198.html
   My bibliography  Save this article

Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics

Author

Listed:
  • Carsten Grashoff

    (Robert M. Berne Cardiovascular Research Center, University of Virginia
    University of Virginia)

  • Brenton D. Hoffman

    (Robert M. Berne Cardiovascular Research Center, University of Virginia
    University of Virginia)

  • Michael D. Brenner

    (University of Illinois at Urbana-Champaign
    University of Illinois at Urbana-Champaign)

  • Ruobo Zhou

    (University of Illinois at Urbana-Champaign)

  • Maddy Parsons

    (King’s College London)

  • Michael T. Yang

    (University of Pennsylvania)

  • Mark A. McLean

    (University of Illinois at Urbana-Champaign)

  • Stephen G. Sligar

    (University of Illinois at Urbana-Champaign)

  • Christopher S. Chen

    (University of Pennsylvania)

  • Taekjip Ha

    (University of Illinois at Urbana-Champaign
    University of Illinois at Urbana-Champaign
    Howard Hughes Medical Institute)

  • Martin A. Schwartz

    (Robert M. Berne Cardiovascular Research Center, University of Virginia
    University of Virginia
    University of Virginia)

Abstract

Intracellular forces defined The ability of cells to respond to physical forces is fundamental to development and physiology, including regulation of blood pressure, cell adhesion and migration. A major limitation to the study of these phenomena has been the difficulty of measuring molecular forces in cells in vivo. Grashoff et al. now report the development of a genetically encoded, fluorescent tension-sensing module capable of measuring mechanical forces across specific proteins in vivo. The sensor was tested on vinculin, a membrane-cytoskeletal protein that is recruited to focal adhesions and connects cell-adhesion molecules (integrins) to actin filaments. The data reveal a regulatory mechanism in which the ability of vinculin to bear force determines whether focal adhesions assemble or disassemble under force. This new biosensor should be applicable to other proteins involved in mechanotransduction.

Suggested Citation

  • Carsten Grashoff & Brenton D. Hoffman & Michael D. Brenner & Ruobo Zhou & Maddy Parsons & Michael T. Yang & Mark A. McLean & Stephen G. Sligar & Christopher S. Chen & Taekjip Ha & Martin A. Schwartz, 2010. "Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics," Nature, Nature, vol. 466(7303), pages 263-266, July.
  • Handle: RePEc:nat:nature:v:466:y:2010:i:7303:d:10.1038_nature09198
    DOI: 10.1038/nature09198
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09198
    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/nature09198?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.

    Citations

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


    Cited by:

    1. Matthew R. Pawlak & Adam T. Smiley & Maria Paz Ramirez & Marcus D. Kelly & Ghaidan A. Shamsan & Sarah M. Anderson & Branden A. Smeester & David A. Largaespada & David J. Odde & Wendy R. Gordon, 2023. "RAD-TGTs: high-throughput measurement of cellular mechanotype via rupture and delivery of DNA tension probes," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Jiankai Wei & Wei Zhang & An Jiang & Hongzhe Peng & Quanyong Zhang & Yuting Li & Jianqing Bi & Linting Wang & Penghui Liu & Jing Wang & Yonghang Ge & Liya Zhang & Haiyan Yu & Lei Li & Shi Wang & Liang, 2024. "Temporospatial hierarchy and allele-specific expression of zygotic genome activation revealed by distant interspecific urochordate hybrids," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. Sorosh Amiri & Camelia Muresan & Xingbo Shang & Clotilde Huet-Calderwood & Martin A. Schwartz & David A. Calderwood & Michael Murrell, 2023. "Intracellular tension sensor reveals mechanical anisotropy of the actin cytoskeleton," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    4. Chrystian Junqueira Alves & Rafael Dariolli & Jonathan Haydak & Sangjo Kang & Theodore Hannah & Robert J. Wiener & Stefanie DeFronzo & Rut Tejero & Gabriele L. Gusella & Aarthi Ramakrishnan & Rodrigo , 2021. "Plexin-B2 orchestrates collective stem cell dynamics via actomyosin contractility, cytoskeletal tension and adhesion," Nature Communications, Nature, vol. 12(1), pages 1-23, December.
    5. Brooke E. Danielsson & Bobin George Abraham & Elina Mäntylä & Jolene I. Cabe & Carl R. Mayer & Anna Rekonen & Frans Ek & Daniel E. Conway & Teemu O. Ihalainen, 2023. "Nuclear lamina strain states revealed by intermolecular force biosensor," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    6. Serena Petracchini & Daniel Hamaoui & Anne Doye & Atef Asnacios & Florian Fage & Elisa Vitiello & Martial Balland & Sebastien Janel & Frank Lafont & Mukund Gupta & Benoit Ladoux & Jerôme Gilleron & Te, 2022. "Optineurin links Hace1-dependent Rac ubiquitylation to integrin-mediated mechanotransduction to control bacterial invasion and cell division," Nature Communications, Nature, vol. 13(1), pages 1-22, December.
    7. Yuhang Zhang & Jingyi Du & Xian Liu & Fei Shang & Yunxin Deng & Jiaqing Ye & Yukai Wang & Jie Yan & Hu Chen & Miao Yu & Shimin Le, 2024. "Multi-domain interaction mediated strength-building in human α-actinin dimers unveiled by direct single-molecule quantification," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    8. Florian Franz & Rafael Tapia-Rojo & Sabina Winograd-Katz & Rajaa Boujemaa-Paterski & Wenhong Li & Tamar Unger & Shira Albeck & Camilo Aponte-Santamaria & Sergi Garcia-Manyes & Ohad Medalia & Benjamin , 2023. "Allosteric activation of vinculin by talin," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    9. Venkat R. Chirasani & Mohammad Ashhar I. Khan & Juilee N. Malavade & Nikolay V. Dokholyan & Brenton D. Hoffman & Sharon L. Campbell, 2023. "Molecular basis and cellular functions of vinculin-actin directional catch bonding," Nature Communications, Nature, vol. 14(1), pages 1-20, 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:nature:v:466:y:2010:i:7303:d:10.1038_nature09198. 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.