ArticleScientific reports2019
Binding partner- and force-promoted changes in αE-catenin conformation probed by native cysteine labeling.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Long-read, whole-genome sequencing and chemotherapy response of two patient-derived organoids from a TP53- and KRAS-mutant ovarian carcinoma.bioRxiv : the preprint server for biology · 2026Article
- α-catenin phosphorylation is actomyosin-sensitive and required for epithelial barrier functions through Afadin.bioRxiv : the preprint server for biology · 2025Article
- α-Catenin force-sensitive binding and sequestration of LZTS2 leads to cytokinesis failure.The Journal of cell biology · 2025Article
- α-catenin middle- and actin-binding domain unfolding mutants differentially impact epithelial strength and sheet migration.Molecular biology of the cell · 2024Article
- α-catenin mechanosensitivity as a route to cytokinesis failure through sequestration of LZTS2.bioRxiv : the preprint server for biology · 2023Article
- Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments.Communications biology · 2023Article
- SRGP-1/srGAP and AFD-1/afadin stabilize HMP-1/⍺-catenin at rosettes to seal internalization sites following gastrulation in C. elegans.PLoS genetics · 2023Article
- Multi-level Force-dependent Allosteric Enhancement of αE-catenin Binding to F-actin by Vinculin.Journal of molecular biology · 2023Article
- The α-Catenin mechanosensing M region is required for cell adhesion during tissue morphogenesis.The Journal of cell biology · 2023Article
- Wild‑type KRAS inhibits the migration and invasion of pancreatic cancer through the Wnt/β‑catenin pathway.Molecular medicine reports · 2023Article
- Article
- Powering morphogenesis: multiscale challenges at the interface of cell adhesion and the cytoskeleton.Molecular biology of the cell · 2022Review
- Activated nanoscale actin-binding domain motion in the catenin-cadherin complex revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Distinct intramolecular interactions regulate autoinhibition of vinculin binding in αT-catenin and αE-catenin.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Adherens Junctions (AJs) are cell-cell adhesion complexes that sense and propagate mechanical forces by coupling cadherins to the actin cytoskeleton via β-catenin and the F-actin binding protein αE-catenin. When subjected to mechanical force, the cadherin•catenin complex can tightly link to F-actin through αE-catenin, and also recruits the F-actin-binding protein vinculin. In this study, labeling of native cysteines combined with mass spectrometry revealed conformational changes in αE-catenin upon binding to the E-cadherin•β-catenin complex, vinculin and F-actin. A method to apply physiologically meaningful forces in solution revealed force-induced conformational changes in αE-catenin when bound to F-actin. Comparisons of wild-type αE-catenin and a mutant with enhanced vinculin affinity using cysteine labeling and isothermal titration calorimetry provide evidence for allosteric coupling of the N-terminal β-catenin-binding and the middle (M) vinculin-binding domain of αE-catenin. Cysteine labeling also revealed possible crosstalk between the actin-binding domain and the rest of the protein. The data provide insight into how binding partners and mechanical stress can regulate the conformation of full-length αE-catenin, and identify the M domain as a key transmitter of conformational changes.
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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.