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Generic self-stabilization mechanism for biomolecular adhesions under load

Author

Listed:
  • Andrea Braeutigam

    (Institute for Biological Information Processes, Forschungszentrum Jülich)

  • Ahmet Nihat Simsek

    (Institute for Biological Information Processes, Forschungszentrum Jülich
    Institute for Infectious Diseases and Zoonoses, Ludwig-Maximilians-Universität München)

  • Gerhard Gompper

    (Institute for Biological Information Processes, Forschungszentrum Jülich)

  • Benedikt Sabass

    (Institute for Biological Information Processes, Forschungszentrum Jülich
    Institute for Infectious Diseases and Zoonoses, Ludwig-Maximilians-Universität München)

Abstract

Mechanical loading generally weakens adhesive structures and eventually leads to their rupture. However, biological systems can adapt to loads by strengthening adhesions, which is essential for maintaining the integrity of tissue and whole organisms. Inspired by cellular focal adhesions, we suggest here a generic, molecular mechanism that allows adhesion systems to harness applied loads for self-stabilization through adhesion growth. The mechanism is based on conformation changes of adhesion molecules that are dynamically exchanged with a reservoir. Tangential loading drives the occupation of some states out of equilibrium, which, for thermodynamic reasons, leads to association of further molecules with the cluster. Self-stabilization robustly increases adhesion lifetimes in broad parameter ranges. Unlike for catch-bonds, bond rupture rates can increase monotonically with force. The self-stabilization principle can be realized in many ways in complex adhesion-state networks; we show how it naturally occurs in cellular adhesions involving the adaptor proteins talin and vinculin.

Suggested Citation

  • Andrea Braeutigam & Ahmet Nihat Simsek & Gerhard Gompper & Benedikt Sabass, 2022. "Generic self-stabilization mechanism for biomolecular adhesions under load," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29823-2
    DOI: 10.1038/s41467-022-29823-2
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    References listed on IDEAS

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    1. R. Dean Astumian, 2019. "Kinetic asymmetry allows macromolecular catalysts to drive an information ratchet," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    2. Huimin Zhang & Frédéric Landmann & Hala Zahreddine & David Rodriguez & Marc Koch & Michel Labouesse, 2011. "A tension-induced mechanotransduction pathway promotes epithelial morphogenesis," Nature, Nature, vol. 471(7336), pages 99-103, March.
    3. Mingxi Yao & Benjamin T. Goult & Benjamin Klapholz & Xian Hu & Christopher P. Toseland & Yingjian Guo & Peiwen Cong & Michael P. Sheetz & Jie Yan, 2016. "The mechanical response of talin," Nature Communications, Nature, vol. 7(1), pages 1-11, September.
    4. Paul Atherton & Ben Stutchbury & De-Yao Wang & Devina Jethwa & Ricky Tsang & Eugenia Meiler-Rodriguez & Pengbo Wang & Neil Bate & Roy Zent & Igor L. Barsukov & Benjamin T. Goult & David R. Critchley &, 2015. "Vinculin controls talin engagement with the actomyosin machinery," Nature Communications, Nature, vol. 6(1), pages 1-12, December.
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    Cited by:

    1. 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.

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