ArticleCell reports2024
Fat-Dachsous planar polarity function requires two distinct heterophilic cadherin-cadherin binding interactions.
Article in Cell reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Research on the role and mechanism of FAT4 in the development and progression of tumor and non-tumor diseases.Discover oncology · 2026Review
- Regulation of Hippo signaling and planar cell polarity via distinct regions of the Fat intracellular domain.Development (Cambridge, England) · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fat and Dachsous are evolutionarily conserved atypical cadherins that regulate polarized cell behaviors. In the Drosophila wing, they interact heterophilically between neighboring cells, localize asymmetrically to opposite cell ends, and control wing shape by regulating oriented cell rearrangements and divisions. Fat and Dachsous have 34 and 27 cadherin repeats, respectively, and previous work has identified trans interactions between their first four cadherin repeats. Here, we identify a second heterophilic binding site in their C-terminal cadherin repeats and show the conservation of this binding site in human Fat4 and Dachsous1. We provide evidence that both N- and C-terminal binding sites regulate the stability of Fat-Dachsous binding interactions and show that the N-terminal binding sites are partly dispensable for Fat-Dachsous function in vivo. Finally, we provide in vivo confirmation that the N-terminal repeats interact in an anti-parallel manner. We propose that multiple binding sites promote the clustering of Fat and Dachsous into a lattice-like array.
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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 Socratic graph.