ArticleCurrent biology : CB2015
Dynamic visualization of α-catenin reveals rapid, reversible conformation switching between tension states.
Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
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Who cites it
95 citing papers in PubMed, 164 citations in OpenAlex.
- De novo E-cadherin/catenin complex formation controls basal epithelial mechanics and force transmission for apoptotic cell clearance.Nature communications · 2026Article
- Cadherin regulation of endoplasmic reticulum-plasma membrane contact sites.Cell reports · 2026Article
- Molecular tension indicators reveal unexpectedly complex regulation of tension in live mouse organs.Communications biology · 2026Article
- Epidermal growth factor receptor is an essential component in E-cadherin force transduction complexes.Journal of cell science · 2025Article
- Actomyosin forces trigger a conformational change in desmoplakin within desmosomes.Nature communications · 2025Article
- A conformational change in α-catenin's actin-binding domain governs adherens junction maturation.Communications biology · 2025Article
- α-catenin phosphorylation is actomyosin-sensitive and required for epithelial barrier functions through Afadin.bioRxiv : the preprint server for biology · 2025Article
- Decoding force-transmission linkages for therapeutic targeting and engineering.APL bioengineering · 2025Review
- α-Catenin force-sensitive binding and sequestration of LZTS2 leads to cytokinesis failure.The Journal of cell biology · 2025Article
- Dysfunctional mechanotransduction regulates the progression of PIK3CA-driven vascular malformations.APL bioengineering · 2025Article
- Cadherins and growth factor receptors - ligand-selective mechano-switches at cadherin junctions.Journal of cell science · 2025Article
- α-catenin phosphorylation is elevated during mitosis to resist apical rounding and epithelial barrier leak.Biology open · 2025Article
- Dysfunctional mechanotransduction regulates the progression of PIK3CA-driven vascular malformations.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
- Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis.Cell reports · 2024Article
- Article
- The ability of the LIMD1 and TRIP6 LIM domains to bind strained f-actin is critical for their tension dependent localization to adherens junctions and association with the Hippo pathway kinase LATS1.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Alternative molecular mechanisms for force transmission at adherens junctions via β-catenin-vinculin interaction.Nature communications · 2024Article
- α-catenin middle- and actin-binding domain unfolding mutants differentially impact epithelial strength and sheet migration.Molecular biology of the cell · 2024Article
- Modelling and targeting mechanical forces in organ fibrosis.Nature reviews bioengineering · 2024Article
35 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The cytosolic protein α-catenin is a postulated force transducer at cadherin complexes. The demonstration of force activation, identification of consequent downstream events in live cells, and development of tools to study these dynamic processes in living cells are central to elucidating the role of α-catenin in cellular mechanics and tissue function. Here we demonstrate that α-catenin is a force-activatable mechanotransducer at cell-cell junctions by using an engineered α-catenin conformation sensor based on fluorescence resonance energy transfer (FRET). This sensor reconstitutes α-catenin-dependent functions in α-catenin-depleted cells and recapitulates the behavior of the endogenous protein. Dynamic imaging of cells expressing the sensor demonstrated that α-catenin undergoes immediate, reversible conformation switching in direct response to different mechanical perturbations of cadherin adhesions. Combined magnetic twisting cytometry with dynamic FRET imaging revealed rapid, local conformation switching upon the mechanical stimulation of specific cadherin bonds. At acutely stretched cell-cell junctions, the immediate, reversible conformation change further reveals that α-catenin behaves like an elastic spring in series with cadherin and actin. The force-dependent recruitment of vinculin—a principal α-catenin effector—to junctions requires the vinculin binding site of the α-catenin sensor. In cells, the relative rates of force-dependent α-catenin conformation switching and vinculin recruitment reveal that α-catenin activation and vinculin recruitment occur sequentially, rather than in a concerted process, with vinculin accumulation being significantly slower. This engineered α-catenin sensor revealed that α-catenin is a reversible, stretch-activatable sensor that mechanically links cadherin complexes and actin and is an indispensable player in cadherin-specific mechanotransduction at intercellular junctions.
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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.