ArticleJournal of cell science2021
Structural variability and dynamics in the ectodomain of an ancestral-type classical cadherin revealed by AFM imaging.
Article in Journal of cell science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- 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
- Powering morphogenesis: multiscale challenges at the interface of cell adhesion and the cytoskeleton.Molecular biology of the cell · 2022Review
- Structural variability and dynamics in the ectodomain of an ancestral-type classical cadherin revealed by AFM imaging.Journal of cell science · 2021Article
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Authors and funding
2 authors.
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Abstract
Type III cadherin represents the ancestral form of classical cadherin in bilaterian metazoans. Drosophila possesses type III and type IVa cadherins, known as DN- and DE-cadherins, respectively. Mature DN- and DE-cadherins have 15 and 7 extracellular cadherin domain (EC) repeats, respectively, with DN-cadherin EC6-EC11 homologous to DE-cadherin EC1-EC6. These EC repeats contain predicted complete or partial Ca2+-free inter-EC linkers that potentially contribute to adhesion. Comparative structure-function studies of DN- and DE-cadherins may help us understand the ancestral and derived states of classical cadherin-mediated adhesion mechanisms. Here, using bead aggregation assays, we found that DN-cadherin EC1-EC11 and DE-cadherin EC1-EC6 exhibit Ca2+-dependent adhesive properties. Using high-speed atomic force microscopy (HS-AFM) imaging in solution, we show that both DN- and DE-cadherin ectodomains share a common morphological framework consisting of a strand-like and a globule-like portion. Furthermore, the DN-cadherin EC repeats are highly variable, flexible in morphology and have at least three bendable sites, one of which is located in EC6-EC11 and can act as a flexible hinge. Our findings provide insights into diversification of classical cadherin-mediated adhesion mechanisms. This article has an associated First Person interview with the first author of the paper.
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