ArticleNature communications2023
Structure of the planar cell polarity cadherins Fat4 and Dachsous1.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- FAT4 restrains epithelial-mesenchymal transition and metastasis in cervical cancer and shapes the tumor immune microenvironment.Journal of translational medicine · 2026Article
- Article
- Single-cell and spatial transcriptomics define 20E-driven developmental reprogramming in silkworm wing disc.Nature communications · 2026Article
- Dynamic Expression and Functional Implications of the Cell Polarity Gene, Dchs1, During Cardiac Development.Cells · 2025Article
- DCHS1 Modulates Forebrain Proportions in Modern Humans via a Glycosylation Change.bioRxiv : the preprint server for biology · 2025Article
- Fat4 intracellular domain controls internalization of Fat4/Dchs1 planar polarity membrane complexes.Biophysical journal · 2025Article
- Interacting Fat1 and Dchs Planar Cell Polarity Proteins Supported by Fjx1 Serve as Heterodimeric Intercellular Bridges Crucial to Support Spermatogenesis.Advances in experimental medicine and biology · 2025Review
- Hippo signaling pathway in cervical cancer: insights into mechanisms and therapeutic potential.Frontiers in oncology · 2025Review
- Emergence of planar cell polarity from the interplay of local interactions and global gradients.eLife · 2024Article
- Fat-Dachsous planar polarity function requires two distinct heterophilic cadherin-cadherin binding interactions.Cell reports · 2024Article
- Chromosome-level genome assembly of Oncomelania hupensis: the intermediate snail host of Schistosoma japonicum.Infectious diseases of poverty · 2024Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The atypical cadherins Fat and Dachsous are key regulators of cell growth and animal development. In contrast to classical cadherins, which form homophilic interactions to segregate cells, Fat and Dachsous cadherins form heterophilic interactions to induce cell polarity within tissues. Here, we determine the co-crystal structure of the human homologs Fat4 and Dachsous1 (Dchs1) to establish the molecular basis for Fat-Dachsous interactions. The binding domains of Fat4 and Dchs1 form an extended interface along extracellular cadherin (EC) domains 1-4 of each protein. Biophysical measurements indicate that Fat4-Dchs1 affinity is among the highest reported for cadherin superfamily members, which is attributed to an extensive network of salt bridges not present in structurally similar protocadherin homodimers. Furthermore, modeling suggests that unusual extracellular phosphorylation modifications directly modulate Fat-Dachsous binding by introducing charged contacts across the interface. Collectively, our analyses reveal how the molecular architecture of Fat4-Dchs1 enables them to form long-range, high-affinity interactions to maintain planar cell polarity.
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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 OpenQuestion graph.