ArticleProceedings of the National Academy of Sciences of the United States of America2023
Antiparallel dimer structure of CELSR cadherin in solution revealed by high-speed atomic force microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Article
- Synaptic Cell Adhesion: A Functional Perspective.Advances in neurobiology · 2026Review
- Cell autonomous polarization by the planar cell polarity signaling pathway.Nature communications · 2025Article
- Cell autonomous polarization by the planar cell polarity signaling pathway.bioRxiv : the preprint server for biology · 2025Article
- Structural basis for regulation of CELSR1 by a compact module in its extracellular region.Nature communications · 2025Article
- Molecular symmetry breaking in the Frizzled-dependent planar polarity pathway.Current biology : CB · 2023Article
- Antiparallel dimer structure of CELSR cadherin in solution revealed by high-speed atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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Authors and funding
3 authors.
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Abstract
Cadherin EGF LAG seven-pass G-type receptors (CELSR) cadherins, members of the cadherin superfamily, and adhesion G-protein-coupled receptors, play a vital role in cell-cell adhesion. The mutual binding of the extracellular domains (ectodomains) of CELSR cadherins between cells is crucial for tissue formation, including the establishment of planar cell polarity, which directs the proper patterning of cells. CELSR cadherins possess nine cadherin ectodomains (EC1-EC9) and noncadherin ectodomains. However, the structural and functional mechanisms of the binding mode of CELSR cadherins have not been determined. In this study, we investigated the binding mode of CELSR cadherins using single-molecule fluorescence microscopy, high-speed atomic force microscopy (HS-AFM), and bead aggregation assay. The fluorescence microscopy analysis results indicated that the
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