ArticleProceedings of the National Academy of Sciences of the United States of America2012
E-cadherin is under constitutive actomyosin-generated tension that is increased at cell-cell contacts upon externally applied stretch.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 343 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
343 citing papers in PubMed, 602 citations in OpenAlex.
- Force-Locking DNA Hairpin Probes for High-Throughput and Cumulative Detection of Intercellular Molecular Tensions.Angewandte Chemie (International ed. in English) · 2026Article
- Biophysics of lumen morphogenesis.Development (Cambridge, England) · 2026Review
- Engineered microtissue systems for identifying the roles of Wnt and YAP signaling in hepatoblast differentiation and organization.Materials today. Bio · 2026Article
- Goblet cells mechanically breach the epithelial barrier in gut homeostasis.Nature communications · 2026Article
- Membrane Tension Integrates Physical and Signaling Cues to Gate Cell Fate Transitions.bioRxiv : the preprint server for biology · 2026Article
- Review
- Mechanical states of a motor protein in the spindle.Current biology : CB · 2026Article
- Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Actomyosin contractility and a threshold of cadherin cell adhesion are required during tissue fusion.The Journal of cell biology · 2026Article
- Mechanotransduction and cell fate: from molecular sensors to multicellular self-organization.Frontiers in cell and developmental biology · 2026Review
- Synthetic mechanoreceptor engineering: From genetic encoding to DNA nanotechnology-based reprogramming.Mechanobiology in medicine · 2025Review
- Article
- Paths to stability - actin regulation of adherens junction mechanics.Journal of cell science · 2025Review
- Epidermal growth factor receptor is an essential component in E-cadherin force transduction complexes.Journal of cell science · 2025Article
- Article
- 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
- Immunological synapse: structures, molecular mechanisms and therapeutic implications in disease.Signal transduction and targeted therapy · 2025Review
- Dynamic Remodeling of Mechano-Sensing Complexes in Suspended Fibroblast Cell-Sheets Under External Mechanical Stimulus.Biotechnology and bioengineering · 2025Article
- Force transmission is a master regulator of mechanical cell competition.Nature materials · 2025Article
- Measuring and manipulating mechanical forces during development.Nature cell biology · 2025Review
283 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Classical cadherins are transmembrane proteins at the core of intercellular adhesion complexes in cohesive metazoan tissues. The extracellular domain of classical cadherins forms intercellular bonds with cadherins on neighboring cells, whereas the cytoplasmic domain recruits catenins, which in turn associate with additional cytoskeleton binding and regulatory proteins. Cadherin/catenin complexes are hypothesized to play a role in the transduction of mechanical forces that shape cells and tissues during development, regeneration, and disease. Whether mechanical forces are transduced directly through cadherins is unknown. To address this question, we used a Förster resonance energy transfer (FRET)-based molecular tension sensor to test the origin and magnitude of tensile forces transmitted through the cytoplasmic domain of E-cadherin in epithelial cells. We show that the actomyosin cytoskeleton exerts pN-tensile force on E-cadherin, and that this tension requires the catenin-binding domain of E-cadherin and αE-catenin. Surprisingly, the actomyosin cytoskeleton constitutively exerts tension on E-cadherin at the plasma membrane regardless of whether or not E-cadherin is recruited to cell-cell contacts, although tension is further increased at cell-cell contacts when adhering cells are stretched. Our findings thus point to a constitutive role of E-cadherin in transducing mechanical forces between the actomyosin cytoskeleton and the plasma membrane, not only at cell-cell junctions but throughout the cell surface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.