ArticleNature communications2024
Alternative molecular mechanisms for force transmission at adherens junctions via β-catenin-vinculin interaction.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Cellular Responses to Mechanical Cues Across Scales: From Fundamental Insights to Translational Potential.Advanced healthcare materials · 2026Review
- A novel, PCP-dependent tissue organising principle coordinating morphogenesis between embryonic skin epidermal layers.Journal of anatomy · 2026Article
- Systematic AI-assisted screening of the cadhesome to map epithelial monolayer mechanics.Cell communication and signaling : CCS · 2026Article
- Single Cell Mechanics in Disease Progression.Small science · 2026Review
- Two δ-catenins, plakophilin 4 and p120, promote formation of distinct types of adherens junctions.The Journal of cell biology · 2026Article
- Actomyosin-dependent assembly of the mechanosensitive machinery from adherens junctions triggers actin polymerization and organization.Science advances · 2026Article
- Article
- Development of three-colour FRET cascade for force sensing of the putative RIAM-vinculin interaction in fibroblasts.Communications chemistry · 2025Article
- Impaired MAPT/tau-secretory lysosomes are linked to cognitive vulnerability in Alzheimer patients.Autophagy · 2025Article
- Paths to stability - actin regulation of adherens junction mechanics.Journal of cell science · 2025Review
- 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
- A conformational change in α-catenin's actin-binding domain governs adherens junction maturation.Communications biology · 2025Article
- Expression profiles of E-cadherin and N-cadherin in endometriosis and other gynecological diseases towards targeted treatment: a systematic review.Obstetrics & gynecology science · 2025Article
- Dynamic GLUT trafficking at high glucose levels enhances insulin secretion: Dysregulation leads to decreased insulin secretion during type 2 diabetes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- E-Cadherin: A conductor of cellular signaling.Current opinion in cell biology · 2025Review
- Dynamic Remodeling of Mechano-Sensing Complexes in Suspended Fibroblast Cell-Sheets Under External Mechanical Stimulus.Biotechnology and bioengineering · 2025Article
- Cadherin dynamics and cortical tension in remodeling cell-cell adhesion during EMT.Biophysical journal · 2025Article
- Visualizing androgen signaling and assessing its interaction with canonical Wnt signaling pathways in prostate development, morphogenesis, and regeneration.PLoS genetics · 2025Article
- Review
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Authors and funding
20 authors.
Funding
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Abstract
Force transmission through adherens junctions (AJs) is crucial for multicellular organization, wound healing and tissue regeneration. Recent studies shed light on the molecular mechanisms of mechanotransduction at the AJs. However, the canonical model fails to explain force transmission when essential proteins of the mechanotransduction module are mutated or missing. Here, we demonstrate that, in absence of α-catenin, β-catenin can directly and functionally interact with vinculin in its open conformation, bearing physiological forces. Furthermore, we found that β-catenin can prevent vinculin autoinhibition in the presence of α-catenin by occupying vinculin´s head-tail interaction site, thus preserving force transmission capability. Taken together, our findings suggest a multi-step force transmission process at AJs, where α-catenin and β-catenin can alternatively and cooperatively interact with vinculin. This can explain the graded responses needed to maintain tissue mechanical homeostasis and, importantly, unveils a force-bearing mechanism involving β-catenin and extended vinculin that can potentially explain the underlying process enabling collective invasion of metastatic cells lacking α-catenin.
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