ArticleProceedings of the National Academy of Sciences of the United States of America2014
Giant cadherins Fat and Dachsous self-bend to organize properly spaced intercellular junctions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 63 citations in OpenAlex.
- Structural basis for regulation of CELSR1 by a compact module in its extracellular region.Nature communications · 2025Article
- Fat-Dachsous planar polarity function requires two distinct heterophilic cadherin-cadherin binding interactions.Cell reports · 2024Article
- Dachsous cadherin related 1 (DCHS1) is a novel biomarker for immune infiltration and epithelial-mesenchymal transition in endometrial cancer via pan-cancer analysis.Journal of ovarian research · 2024Article
- Fat2 polarizes Lar and Sema5c to coordinate the motility of collectively migrating epithelial cells.Journal of cell science · 2024Article
- Modulation of a conformational ensemble by a small molecule that inhibits key protein-protein interactions involved in cell adhesion.Protein science : a publication of the Protein Society · 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
- Fat2 polarizes Lar and Sema5c to coordinate the motility of collectively migrating epithelial cells.bioRxiv : the preprint server for biology · 2023Article
- Structure of the planar cell polarity cadherins Fat4 and Dachsous1.Nature communications · 2023Article
- Sculpting an Embryo: The Interplay between Mechanical Force and Cell Division.Journal of developmental biology · 2022Review
- Collective mechanical responses of cadherin-based adhesive junctions as predicted by simulations.Biophysical journal · 2022Article
- Structural variability and dynamics in the ectodomain of an ancestral-type classical cadherin revealed by AFM imaging.Journal of cell science · 2021Article
- Review
- Cadherins down-regulation: towards a better understanding of their relevance in colorectal cancer.Histology and histopathology · 2020Review
- Structural determinants of protocadherin-15 mechanics and function in hearing and balance perception.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Atypical cadherin FAT4 orchestrates lymphatic endothelial cell polarity in response to flow.The Journal of clinical investigation · 2020Article
- Cadherins, Selectins, and Integrins in CAM-DR in Leukemia.Frontiers in oncology · 2020Review
- Structural basis of the strong cell-cell junction formed by cadherin-23.The FEBS journal · 2019Article
- The strong propensity of Cadherin-23 for aggregation inhibits cell migration.Molecular oncology · 2019Article
- Reduced SERCA Function Preferentially Affects Wnt Signaling by Retaining E-Cadherin in the Endoplasmic Reticulum.Cell reports · 2019Article
- A Mechanically Weak Extracellular Membrane-Adjacent Domain Induces Dimerization of Protocadherin-15.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cadherins Fat and Dachsous regulate cell polarity and proliferation via their heterophilic interactions at intercellular junctions. Their ectodomains are unusually large because of repetitive extracellular cadherin (EC) domains, which raises the question of how they fit in regular intercellular spaces. Cadherins typically exhibit a linear topology through the binding of Ca(2+) to the linker between the EC domains. Our electron-microscopic observations of mammalian Fat4 and Dachsous1 ectodomains, however, revealed that, although their N-terminal regions exhibit a linear configuration, the C-terminal regions are kinked with multiple hairpin-like bends. Notably, certain EC-EC linkers in Fat4 and Dachsous1 lost Ca(2+)-binding amino acids. When such non-Ca(2+)-binding linkers were substituted for a normal linker in E-cadherin, the mutant E-cadherins deformed more extensively than the wild-type molecule. To simulate cadherin structures with non-Ca(2+)-binding linkers, we used an elastic network model and confirmed that bent configurations can be generated by deformation of non-Ca(2+)-binding linkers. These findings suggest that Fat and Dachsous self-bend due to the loss of Ca(2+)-binding amino acids from specific EC-EC linkers, and can therefore adapt to confined spaces.
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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 OpenQuestion graph.