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Vinculin controls talin engagement with the actomyosin machinery

Author

Listed:
  • Paul Atherton

    (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)

  • Ben Stutchbury

    (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)

  • De-Yao Wang

    (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)

  • Devina Jethwa

    (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)

  • Ricky Tsang

    (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)

  • Eugenia Meiler-Rodriguez

    (Complutense, University of Madrid)

  • Pengbo Wang

    (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)

  • Neil Bate

    (University of Leicester)

  • Roy Zent

    (Vanderbilt Centre for Kidney Disease, S-3223 Medical Centre)

  • Igor L. Barsukov

    (Institute of Integrative Biology, University of Liverpool)

  • Benjamin T. Goult

    (School of Biosciences, University of Kent)

  • David R. Critchley

    (University of Leicester)

  • Christoph Ballestrem

    (Wellcome Trust Centre for Cell-Matrix Research, University of Manchester)

Abstract

The link between extracellular-matrix-bound integrins and intracellular F-actin is essential for cell spreading and migration. Here, we demonstrate how the actin-binding proteins talin and vinculin cooperate to provide this link. By expressing structure-based talin mutants in talin null cells, we show that while the C-terminal actin-binding site (ABS3) in talin is required for adhesion complex assembly, the central ABS2 is essential for focal adhesion (FA) maturation. Thus, although ABS2 mutants support cell spreading, the cells lack FAs, fail to polarize and exert reduced force on the surrounding matrix. ABS2 is inhibited by the preceding mechanosensitive vinculin-binding R3 domain, and deletion of R2R3 or expression of constitutively active vinculin generates stable force-independent FAs, although cell polarity is compromised. Our data suggest a model whereby force acting on integrin-talin complexes via ABS3 promotes R3 unfolding and vinculin binding, activating ABS2 and locking talin into an actin-binding configuration that stabilizes FAs.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10038
    DOI: 10.1038/ncomms10038
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    Cited by:

    1. 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.
    2. 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.
    3. 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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