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Talin dissociates from RIAM and associates to vinculin sequentially in response to the actomyosin force

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  • Clémence Vigouroux

    (Institute for Integrative Biology of the Cell (I2BC))

  • Véronique Henriot

    (Institute for Integrative Biology of the Cell (I2BC))

  • Christophe Le Clainche

    (Institute for Integrative Biology of the Cell (I2BC))

Abstract

Cells reinforce adhesion strength and cytoskeleton anchoring in response to the actomyosin force. The mechanical stretching of talin, which exposes cryptic vinculin-binding sites, triggers this process. The binding of RIAM to talin could regulate this mechanism. However, the mechanosensitivity of the talin-RIAM complex has never been tested. It is also not known whether RIAM controls the mechanosensitivity of the talin-vinculin complex. To address these issues, we designed an in vitro microscopy assay with purified proteins in which the actomyosin force controls RIAM and vinculin-binding to talin. We demonstrate that actomyosin triggers RIAM dissociation from several talin domains. Actomyosin also provokes the sequential exchange of RIAM for vinculin on talin. The effect of RIAM on this force-dependent binding of vinculin to talin varies from one talin domain to another. This mechanism could allow talin to biochemically code a wide range of forces by selecting different combinations of partners.

Suggested Citation

  • Clémence Vigouroux & Véronique Henriot & Christophe Le Clainche, 2020. "Talin dissociates from RIAM and associates to vinculin sequentially in response to the actomyosin force," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16922-1
    DOI: 10.1038/s41467-020-16922-1
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    Cited by:

    1. Hong Wang & Rayan Said & Clémence Nguyen-Vigouroux & Véronique Henriot & Peter Gebhardt & Julien Pernier & Robert Grosse & Christophe Le Clainche, 2024. "Talin and vinculin combine their activities to trigger actin assembly," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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