ArticleBiophysical journal2023
An ensemble of cadherin-catenin-vinculin complex employs vinculin as the major F-actin binding mode.
Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Conformational flexibility of talin enables force-free sampling of activation-competent states.Communications chemistry · 2026Article
- Role of vinculin in the structural dynamics of cadherin-catenin complexes and its implications for F-actin binding.Protein science : a publication of the Protein Society · 2025Article
- The role of cell junctions in atherosclerosis: implications for inflammation, endothelial dysfunction, and plaque stability.Journal of physiology and biochemistry · 2025Review
- E-Cadherin: A conductor of cellular signaling.Current opinion in cell biology · 2025Review
- Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature.Science advances · 2025Article
- Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature.bioRxiv : the preprint server for biology · 2024Article
- Nanoscale dynamics of the cadherin-catenin complex bound to vinculin revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Adaptable SEC-SAXS data collection for higher quality structure analysis in solution.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
7 authors at 5 institutions in 2 countries.
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Abstract
The cell-cell adhesion cadherin-catenin complexes recruit vinculin to the adherens junction (AJ) to modulate the mechanical couplings between neighboring cells. However, it is unclear how vinculin influences the AJ structure and function. Here, we identified two patches of salt bridges that lock vinculin in the head-tail autoinhibited conformation and reconstituted the full-length vinculin activation mimetics bound to the cadherin-catenin complex. The cadherin-catenin-vinculin complex contains multiple disordered linkers and is highly dynamic, which poses a challenge for structural studies. We determined the ensemble conformation of this complex using small-angle x-ray and selective deuteration/contrast variation small-angle neutron scattering. In the complex, both α-catenin and vinculin adopt an ensemble of flexible conformations, but vinculin has fully open conformations with the vinculin head and actin-binding tail domains well separated from each other. F-actin binding experiments show that the cadherin-catenin-vinculin complex binds and bundles F-actin. However, when the vinculin actin-binding domain is removed from the complex, only a minor fraction of the complex binds to F-actin. The results show that the dynamic cadherin-catenin-vinculin complex employs vinculin as the primary F-actin binding mode to strengthen AJ-cytoskeleton interactions.
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