ArticleProceedings of the National Academy of Sciences of the United States of America2012
Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca²+-free interdomain linkers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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
26 citing papers in PubMed, 42 citations in OpenAlex.
- Two δ-catenins, plakophilin 4 and p120, promote formation of distinct types of adherens junctions.The Journal of cell biology · 2026Article
- 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
- Elastic versus brittle mechanical responses predicted for dimeric cadherin complexes.Biophysical journal · 2022Article
- Heterophilic and homophilic cadherin interactions in intestinal intermicrovillar links are species dependent.PLoS biology · 2021Article
- Mechanism of dimerization and structural features of human LI-cadherin.The Journal of biological chemistry · 2021Article
- Structural variability and dynamics in the ectodomain of an ancestral-type classical cadherin revealed by AFM imaging.Journal of cell science · 2021Article
- 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
- Adhesion Protein Structure, Molecular Affinities, and Principles of Cell-Cell Recognition.Cell · 2020Review
- Nanomechanics of tip-link cadherins.Scientific reports · 2019Article
- Reduced SERCA Function Preferentially Affects Wnt Signaling by Retaining E-Cadherin in the Endoplasmic Reticulum.Cell reports · 2019Article
- Article
- Beyond Cell-Cell Adhesion: Sensational Cadherins for Hearing and Balance.Cold Spring Harbor perspectives in biology · 2018Review
- Evolutionary origin of type IV classical cadherins in arthropods.BMC evolutionary biology · 2017Article
- A Partial Calcium-Free Linker Confers Flexibility to Inner-Ear Protocadherin-15.Structure (London, England : 1993) · 2017Article
- An elastic element in the protocadherin-15 tip link of the inner ear.Nature communications · 2016Article
- Article
- Cadherin flexibility provides a key difference between desmosomes and adherens junctions.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Zebrafish calsyntenins mediate homophilic adhesion through their amino-terminal cadherin repeats.Neuroscience · 2015Article
- Giant cadherins Fat and Dachsous self-bend to organize properly spaced intercellular junctions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Sorting out a promiscuous superfamily: towards cadherin connectomics.Trends in cell biology · 2014Review
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Vertebrate classical cadherins mediate selective calcium-dependent cell adhesion by mechanisms now understood at the atomic level. However, structures and adhesion mechanisms of cadherins from invertebrates, which are highly divergent yet function in similar roles, remain unknown. Here we present crystal structures of three- and four-tandem extracellular cadherin (EC) domain segments from Drosophila N-cadherin (DN-cadherin), each including the predicted N-terminal EC1 domain (denoted EC1') of the mature protein. While the linker regions for the EC1'-EC2' and EC3'-EC4' pairs display binding of three Ca(2+) ions similar to that of vertebrate cadherins, domains EC2' and EC3' are joined in a "kinked" orientation by a previously uncharacterized Ca(2+)-free linker. Biophysical analysis demonstrates that a construct containing the predicted N-terminal nine EC domains of DN-cadherin forms homodimers with affinity similar to vertebrate classical cadherins, whereas deleting the ninth EC domain ablates dimerization. These results suggest that, unlike their vertebrate counterparts, invertebrate cadherins may utilize multiple EC domains to form intercellular adhesive bonds. Sequence analysis reveals that similar Ca(2+)-free linkers are widely distributed in the ectodomains of both vertebrate and invertebrate cadherins.
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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.