ArticleProceedings of the National Academy of Sciences of the United States of America2019
An ensemble of flexible conformations underlies mechanotransduction by the cadherin-catenin adhesion complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Conformational flexibility of talin enables force-free sampling of activation-competent states.Communications chemistry · 2026Article
- β-catenin condensation facilitates clustering of the cadherin/catenin complex and formation of nascent cell-cell junctions.Nature communications · 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
- α-catenin phosphorylation is actomyosin-sensitive and required for epithelial barrier functions through Afadin.bioRxiv : the preprint server for biology · 2025Article
- Beyond Static Tethering at Membrane Contact Sites: Structural Dynamics and Functional Implications of VAP Proteins.Molecules (Basel, Switzerland) · 2025Review
- N-cadherin crosstalk with integrin weakens the molecular clutch in response to surface viscosity.Nature communications · 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
- Structural characterization of an intrinsically disordered protein complex using integrated small-angle neutron scattering and computing.Protein science : a publication of the Protein Society · 2023Article
- An ensemble of cadherin-catenin-vinculin complex employs vinculin as the major F-actin binding mode.Biophysical journal · 2023Article
- Article
- Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments.Communications biology · 2023Article
- The α-Catenin mechanosensing M region is required for cell adhesion during tissue morphogenesis.The Journal of cell biology · 2023Article
- Powering morphogenesis: multiscale challenges at the interface of cell adhesion and the cytoskeleton.Molecular biology of the cell · 2022Review
- Small-angle neutron scattering contrast variation studies of biological complexes: Challenges and triumphs.Current opinion in structural biology · 2022Review
- Reconstitution of the full transmembrane cadherin-catenin complex.Protein expression and purification · 2022Article
- HIV-1-Mediated Acceleration of Oncovirus-Related Non-AIDS-Defining Cancers.Biomedicines · 2022Review
- Intrinsically disordered proteins play diverse roles in cell signaling.Cell communication and signaling : CCS · 2022Review
- DENSS-multiple: A structure reconstruction method using contrast variation of small-angle neutron scattering based on the DENSS algorithm.BBA advances · 2022Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
The cadherin-catenin adhesion complex is the central component of the cell-cell adhesion adherens junctions that transmit mechanical stress from cell to cell. We have determined the nanoscale structure of the adherens junction complex formed by the α-catenin•β-catenin•epithelial cadherin cytoplasmic domain (ABE) using negative stain electron microscopy, small-angle X-ray scattering, and selective deuteration/small-angle neutron scattering. The ABE complex is highly pliable and displays a wide spectrum of flexible structures that are facilitated by protein-domain motions in α- and β-catenin. Moreover, the 107-residue intrinsically disordered N-terminal segment of β-catenin forms a flexible "tongue" that is inserted into α-catenin and participates in the assembly of the ABE complex. The unanticipated ensemble of flexible conformations of the ABE complex suggests a dynamic mechanism for sensitivity and reversibility when transducing mechanical signals, in addition to the catch/slip bond behavior displayed by the ABE complex under mechanical tension. Our results provide mechanistic insight into the structural dynamics for the cadherin-catenin adhesion complex in mechanotransduction.
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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 Socratic graph.