ArticlePNAS nexus2022
Regulation of multiple dimeric states of E-cadherin by adhesion activating antibodies revealed through Cryo-EM and X-ray crystallography.
Article in PNAS nexus, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- O-Mannose Glycosylations Influence E-Cadherin Functional Interactions.Molecular & cellular proteomics : MCP · 2026Article
- Two δ-catenins, plakophilin 4 and p120, promote formation of distinct types of adherens junctions.The Journal of cell biology · 2026Article
- Paths to stability - actin regulation of adherens junction mechanics.Journal of cell science · 2025Review
- Distinct VE-cadherin serine and tyrosine phosphorylation sites and their role for inflammation-induced vascular permeability in vivo.Cellular and molecular life sciences : CMLS · 2025Article
- Outside-in engineering of cadherin endocytosis using a conformation strengthening antibody.Nature communications · 2025Article
- Observation of E-cadherin adherens junction dynamics with metal-induced energy transfer imaging and spectroscopy.Communications biology · 2024Article
- Mesenchymal stromal cells with chimaeric antigen receptors for enhanced immunosuppression.Nature biomedical engineering · 2024Article
- Strengthening E-cadherin adhesion via antibody-mediated binding stabilization.Structure (London, England : 1993) · 2024Article
- Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- Autocorrelation analysis for cryo-EM with sparsity constraints: Improved sample complexity and projection-based algorithms.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- 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
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
E-cadherin adhesion is regulated at the cell surface, a process that can be replicated by activating antibodies. We use cryo-electron microscopy (EM) and X-ray crystallography to examine functional states of the cadherin adhesive dimer. This dimer is mediated by N-terminal beta strand-swapping involving Trp2, and forms via a different transient X-dimer intermediate. X-dimers are observed in cryo-EM along with monomers and strand-swap dimers, indicating that X-dimers form stable interactions. A novel EC4-mediated dimer was also observed. Activating Fab binding caused no gross structural changes in E-cadherin monomers, but can facilitate strand swapping. Moreover, activating Fab binding is incompatible with the formation of the X-dimer. Both cryo-EM and X-ray crystallography reveal a distinctive twisted strand-swap dimer conformation caused by an outward shift in the N-terminal beta strand that may represent a strengthened state. Thus, regulation of adhesion involves changes in cadherin dimer configurations.
Identifiers
What OpenQuestion holds
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.