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Talin and vinculin combine their activities to trigger actin assembly. | LitMetric

AI Article Synopsis

  • Focal adhesions (FAs) enhance their grip on the actin cytoskeleton to withstand force, and the interaction between talin and vinculin plays a key role in this process by influencing actin polymerization.* -
  • Researchers combined various techniques, including TIRF microscopy and kinetic assays, to study how talin and vinculin mutants that simulate mechanical stretching promote a sequence of actin filament activities, including nucleation and elongation.* -
  • Experiments in cells showed that these talin and vinculin mutants led to quicker growth of stress fibers, indicating a flexible mechanism for controlling actin assembly in FAs responding to different biochemical and mechanical signals.*

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11532549PMC
http://dx.doi.org/10.1038/s41467-024-53859-1DOI Listing

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