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The mechanical response of talin

Author

Listed:
  • Mingxi Yao

    (Mechanobiology Institute, National University of Singapore)

  • Benjamin T. Goult

    (School of Biosciences, University of Kent)

  • Benjamin Klapholz

    (Wellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge
    Development and Neuroscience, University of Cambridge)

  • Xian Hu

    (Mechanobiology Institute, National University of Singapore)

  • Christopher P. Toseland

    (School of Biosciences, University of Kent)

  • Yingjian Guo

    (Mechanobiology Institute, National University of Singapore)

  • Peiwen Cong

    (Mechanobiology Institute, National University of Singapore)

  • Michael P. Sheetz

    (Mechanobiology Institute, National University of Singapore
    Columbia University)

  • Jie Yan

    (Mechanobiology Institute, National University of Singapore
    National University of Singapore
    Centre for Bioimaging Sciences, National University of Singapore)

Abstract

Talin, a force-bearing cytoplasmic adapter essential for integrin-mediated cell adhesion, links the actin cytoskeleton to integrin-based cell–extracellular matrix adhesions at the plasma membrane. Its C-terminal rod domain, which contains 13 helical bundles, plays important roles in mechanosensing during cell adhesion and spreading. However, how the structural stability and transition kinetics of the 13 helical bundles of talin are utilized in the diverse talin-dependent mechanosensing processes remains poorly understood. Here we report the force-dependent unfolding and refolding kinetics of all talin rod domains. Using experimentally determined kinetics parameters, we determined the dynamics of force fluctuation during stretching of talin under physiologically relevant pulling speeds and experimentally measured extension fluctuation trajectories. Our results reveal that force-dependent stochastic unfolding and refolding of talin rod domains make talin a very effective force buffer that sets a physiological force range of only a few pNs in the talin-mediated force transmission pathway.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11966
    DOI: 10.1038/ncomms11966
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    Cited by:

    1. 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.
    2. 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.
    3. Sawako Yamashiro & David M. Rutkowski & Kelli Ann Lynch & Ying Liu & Dimitrios Vavylonis & Naoki Watanabe, 2023. "Force transmission by retrograde actin flow-induced dynamic molecular stretching of Talin," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    4. Maximilian Huber & Javier Casares-Arias & Reinhard Fässler & Daniel J. Müller & Nico Strohmeyer, 2023. "In mitosis integrins reduce adhesion to extracellular matrix and strengthen adhesion to adjacent cells," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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