ArticleDevelopmental cell2015
A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo.
Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- F-actin organization excludes E-cadherin from the division furrow to ensure cytokinesis fidelity.Life science alliance · 2026Article
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- TP63 mediates the generation of tumour-specific chromatin loops that underlie MYC activation in radiation-induced tumorigenesis.Nature communications · 2025Article
- Dynamics and functions of E-cadherin complexes in epithelial cell and tissue morphogenesis.Marine life science & technology · 2023Review
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- Game of Tissues: How the Epidermis ThronesJournal of developmental biology · 2020Review
- Inverse docking based screening and identification of protein targets for Cassiarin alkaloids againstSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018Article
- Cell-cell adhesion in metazoans relies on evolutionarily conserved features of the α-catenin·β-catenin-binding interface.The Journal of biological chemistry · 2017Article
- Integration of Cadherin Adhesion and Cytoskeleton atCold Spring Harbor perspectives in biology · 2017Review
- Structural and functional characterization ofThe Journal of biological chemistry · 2017Article
- Phosphorylation potential ofDevelopment (Cambridge, England) · 2017Article
- Characterization of the Cadherin-Catenin Complex of the Sea Anemone Nematostella vectensis and Implications for the Evolution of Metazoan Cell-Cell Adhesion.Molecular biology and evolution · 2016Article
- Regulating cell-cell junctions from A to Z.The Journal of cell biology · 2016Article
- Phosphoregulation of the C. elegans cadherin-catenin complex.The Biochemical journal · 2015Article
- Getting to the core of cadherin complex function in Caenorhabditis elegans.F1000Research · 2015Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
In metazoan adherens junctions, β-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein α-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for β-catenin and promotes cell-cell adhesion in cell culture systems, but its importance has not been demonstrated in vivo. Here, we identify a critical phosphorylated serine in the C. elegans cadherin HMR-1 required for strong binding to the β-catenin homolog HMP-2. Ablation of this phosphoserine interaction produces developmental defects that resemble full loss-of-function (Hammerhead and Humpback) phenotypes. Most metazoans possess a single gene for β-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous β-catenins; for example, C. elegans HMP-2 functions only in cell-cell adhesion, whereas SYS-1 mediates transcriptional activation through interactions with POP-1/Tcf. Our structural data define critical sequence differences responsible for the unique ligand specificities of these two proteins.
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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.