ArticleNature communications2018
Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 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.
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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
68 citing papers in PubMed, 105 citations in OpenAlex.
- 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
- Review
- Paths to stability - actin regulation of adherens junction mechanics.Journal of cell science · 2025Review
- 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
- α-Catenin force-sensitive binding and sequestration of LZTS2 leads to cytokinesis failure.The Journal of cell biology · 2025Article
- Actin-dependent α-catenin oligomerization contributes to adherens junction assembly.Nature communications · 2025Article
- Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature.Science advances · 2025Article
- Analytical methods in studying cell force sensing: principles, current technologies and perspectives.Regenerative biomaterials · 2025Review
- Regulation of epithelial cell jamming transition by cytoskeleton and cell-cell interactions.Biophysics reviews · 2024Review
- Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature.bioRxiv : the preprint server for biology · 2024Article
- Pushing boundaries: mechanisms enabling bacterial pathogens to spread between cells.Infection and immunity · 2024Review
- Confinement promotes nematic alignment of spindle-shaped cells during Drosophila embryogenesis.Development (Cambridge, England) · 2024Article
- α-catenin middle- and actin-binding domain unfolding mutants differentially impact epithelial strength and sheet migration.Molecular biology of the cell · 2024Article
- Adherens junctions as molecular regulators of emergent tissue mechanics.Nature reviews. Molecular cell biology · 2024Review
- Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024Article
- Age-Related RPE changes in Wildtype C57BL/6J Mice between 2 and 32 Months.bioRxiv : the preprint server for biology · 2024Article
- Vinculin is essential for sustaining normal levels of endogenous forces at cell-cell contacts.Biophysical journal · 2023Article
- E-cadherin adhesion dynamics as revealed by an accelerated force ramp are dependent upon the presence of α-catenin.Biochemical and biophysical research communications · 2023Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 5 institutions in 3 countries.
Funding
Abstract
α-catenin is a key mechanosensor that forms force-dependent interactions with F-actin, thereby coupling the cadherin-catenin complex to the actin cytoskeleton at adherens junctions (AJs). However, the molecular mechanisms by which α-catenin engages F-actin under tension remained elusive. Here we show that the α1-helix of the α-catenin actin-binding domain (αcat-ABD) is a mechanosensing motif that regulates tension-dependent F-actin binding and bundling. αcat-ABD containing an α1-helix-unfolding mutation (H1) shows enhanced binding to F-actin in vitro. Although full-length α-catenin-H1 can generate epithelial monolayers that resist mechanical disruption, it fails to support normal AJ regulation in vivo. Structural and simulation analyses suggest that α1-helix allosterically controls the actin-binding residue V796 dynamics. Crystal structures of αcat-ABD-H1 homodimer suggest that α-catenin can facilitate actin bundling while it remains bound to E-cadherin. We propose that force-dependent allosteric regulation of αcat-ABD promotes dynamic interactions with F-actin involved in actin bundling, cadherin clustering, and AJ remodeling during tissue morphogenesis.
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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.