ArticleProceedings of the National Academy of Sciences of the United States of America2016
Molecular determinants of cadherin ideal bond formation: Conformation-dependent unbinding on a multidimensional landscape.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- A computational study for understanding the impact of p120-catenin on the cis-dimerization of cadherin.Journal of molecular cell biology · 2024Article
- Strengthening E-cadherin adhesion via antibody-mediated binding stabilization.Structure (London, England : 1993) · 2024Article
- Push-pull mechanics of E-cadherin ectodomains in biomimetic adhesions.Biophysical journal · 2023Article
- Characterizing interactions in E-cadherin assemblages.Biophysical journal · 2023Article
- Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Wordom update 2: A user-friendly program for the analysis of molecular structures and conformational ensembles.Computational and structural biotechnology journal · 2023Article
- Regulation of multiple dimeric states of E-cadherin by adhesion activating antibodies revealed through Cryo-EM and X-ray crystallography.PNAS nexus · 2022Article
- Molecular mechanism for strengthening E-cadherin adhesion using a monoclonal antibody.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multiple dimeric structures and strand-swap dimerization of E-cadherin in solution visualized by high-speed atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cadherins can dimerize via asymmetric interactions.FEBS letters · 2022Article
- Elastic versus brittle mechanical responses predicted for dimeric cadherin complexes.Biophysical journal · 2022Article
- Using Surface Hydrophobicity Together with Empirical Potentials to Identify Protein-Protein Binding Sites: Application to the Interactions of E-cadherins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Inside-out regulation of E-cadherin conformation and adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cell-cell interfaces as specialized compartments directing cell function.Nature reviews. Molecular cell biology · 2020Review
- Direct visualization of the extracellular binding structure of E-cadherins in liquid.Scientific reports · 2020Article
- Single-molecule studies of classical and desmosomal cadherin adhesion.Current opinion in biomedical engineering · 2019Article
- Structural basis of the strong cell-cell junction formed by cadherin-23.The FEBS journal · 2019Article
- Structure-Based Virtual Screening Allows the Identification of Efficient Modulators of E-Cadherin-Mediated Cell-Cell Adhesion.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Classical cadherin cell-cell adhesion proteins are essential for the formation and maintenance of tissue structures; their primary function is to physically couple neighboring cells and withstand mechanical force. Cadherins from opposing cells bind in two distinct trans conformations: strand-swap dimers and X-dimers. As cadherins convert between these conformations, they form ideal bonds (i.e., adhesive interactions that are insensitive to force). However, the biophysical mechanism for ideal bond formation is unknown. Here, we integrate single-molecule force measurements with coarse-grained and atomistic simulations to resolve the mechanistic basis for cadherin ideal bond formation. Using simulations, we predict the energy landscape for cadherin adhesion, the transition pathways for interconversion between X-dimers and strand-swap dimers, and the cadherin structures that form ideal bonds. Based on these predictions, we engineer cadherin mutants that promote or inhibit ideal bond formation and measure their force-dependent kinetics using single-molecule force-clamp measurements with an atomic force microscope. Our data establish that cadherins adopt an intermediate conformation as they shuttle between X-dimers and strand-swap dimers; pulling on this conformation induces a torsional motion perpendicular to the pulling direction that unbinds the proteins and forms force-independent ideal bonds. Torsional motion is blocked when cadherins associate laterally in a cis orientation, suggesting that ideal bonds may play a role in mechanically regulating cadherin clustering on cell surfaces.
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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.