ArticleCurrent biology : CB2021
P120 catenin potentiates constitutive E-cadherin dimerization at the plasma membrane and regulates trans binding.
Article in Current biology : CB, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- O-Mannose Glycosylations Influence E-Cadherin Functional Interactions.Molecular & cellular proteomics : MCP · 2026Article
- Two δ-catenins, plakophilin 4 and p120, promote formation of distinct types of adherens junctions.The Journal of cell biology · 2026Article
- Free apical surface hetero-cellular CDH1 homophilic binding is a major mediator of blastocyst-endometrium interaction in humans.Human reproduction (Oxford, England) · 2026Article
- β-catenin condensation facilitates clustering of the cadherin/catenin complex and formation of nascent cell-cell junctions.Nature communications · 2025Article
- Intensity-Based Estimation of Monomeric Brightness for Fluorescent Proteins.International journal of molecular sciences · 2025Article
- Epidermal growth factor receptor is an essential component in E-cadherin force transduction complexes.Journal of cell science · 2025Article
- E- and N-cadherin drive hepatic polarity and lumen elongation via opposing effects on RhoA activity.bioRxiv : the preprint server for biology · 2025Article
- A computational study for understanding the impact of p120-catenin on the cis-dimerization of cadherin.Journal of molecular cell biology · 2024Article
- Computational and experimental approaches to quantify protein binding interactions under confinement.Biophysical journal · 2024Review
- Functions of p120-catenin in physiology and diseases.Frontiers in molecular biosciences · 2024Review
- Integrating shear flow and trypsin treatment to assess cell adhesion strength.Biointerphases · 2023Article
- Dynamics and functions of E-cadherin complexes in epithelial cell and tissue morphogenesis.Marine life science & technology · 2023Review
- Degradation of p0071 and p120-catenin during adherens junction disassembly byFrontiers in cellular and infection microbiology · 2023Article
- Cadherins and catenins in cancer: connecting cancer pathways and tumor microenvironment.Frontiers in cell and developmental biology · 2023Review
- Regulation of multiple dimeric states of E-cadherin by adhesion activating antibodies revealed through Cryo-EM and X-ray crystallography.PNAS nexus · 2022Article
- Reconstitution of the full transmembrane cadherin-catenin complex.Protein expression and purification · 2022Article
- Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor-dependent signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Microscopic Visualization of Cell-Cell Adhesion Complexes at Micro and Nanoscale.Frontiers in cell and developmental biology · 2022Review
- Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cadherins are essential adhesion proteins that regulate tissue cohesion and paracellular permeability by assembling dense adhesion plaques at cell-to-cell contacts. Adherens junctions are central to a wide range of tissue functions; identifying protein interactions that potentiate their assembly and regulation has been the focus of research for over 2 decades. Here, we present evidence for a new, unexpected mechanism of cadherin oligomerization on cells. Fully quantified spectral imaging fluorescence resonance energy transfer (FSI-FRET) and fluorescence intensity fluctuation (FIF) measurements directly demonstrate that E-cadherin forms constitutive lateral (cis) dimers at the plasma membrane. Results further show that binding of the cytosolic protein p120ctn binding to the intracellular region is required for constitutive E-cadherin dimerization. This finding differs from a model that attributes lateral (cis) cadherin oligomerization solely to extracellular domain interactions. The present, novel findings are further supported by studies of E-cadherin mutants that uncouple p120ctn binding or with cells in which p120ctn was knocked out using CRISPR-Cas9. Quantitative affinity measurements further demonstrate that uncoupling p120ctn binding reduces the cadherin trans binding affinity and cell adhesion. These findings transform the current model of cadherin assembly at cell surfaces and identify the core building blocks of cadherin-mediated intercellular adhesions. They also identify a new role for p120ctn and reconcile findings that implicate both the extracellular and intracellular cadherin domains in cadherin clustering and intercellular cohesion.
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What OpenQuestion holds
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.