Talin and vinculin combine their activities to trigger actin assembly

Hong Wang, Rayan Said, Clémence Nguyen-Vigouroux, Véronique Henriot, Peter Gebhardt, Julien Pernier, Robert Grosse and Christophe Le Clainche ()
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Hong Wang: Institute for Integrative Biology of the Cell (I2BC)
Rayan Said: Institute for Integrative Biology of the Cell (I2BC)
Clémence Nguyen-Vigouroux: Institute for Integrative Biology of the Cell (I2BC)
Véronique Henriot: Institute for Integrative Biology of the Cell (I2BC)
Peter Gebhardt: University of Freiburg
Julien Pernier: Institute for Integrative Biology of the Cell (I2BC)
Robert Grosse: University of Freiburg
Christophe Le Clainche: Institute for Integrative Biology of the Cell (I2BC)

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract Focal adhesions (FAs) strengthen their link with the actin cytoskeleton to resist force. Talin-vinculin association could reinforce actin anchoring to FAs by controlling actin polymerization. However, the actin polymerization activity of the talin-vinculin complex is not known because it requires the reconstitution of the mechanical and biochemical activation steps that control the association of talin and vinculin. By combining kinetic and binding assays with single actin filament observations in TIRF microscopy, we show that the association of talin and vinculin mutants, mimicking mechanically stretched talin and activated vinculin, triggers a sequential mechanism in which filaments are nucleated, capped and released to elongate. In agreement with these observations, FRAP experiments in cells co-expressing the same constitutive mutants of talin and vinculin revealed accelerated growth of stress fibers. Our findings suggest a versatile mechanism for the regulation of actin assembly in FAs subjected to various combinations of biochemical and mechanical cues.

Date: 2024
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DOI: 10.1038/s41467-024-53859-1

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