ArticleThe Journal of cell biology1999
Functional domains of alpha-catenin required for the strong state of cadherin-based cell adhesion.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
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Who cites it
108 citing papers in PubMed, 255 citations in OpenAlex.
- Context-dependent interactions among afadin, ZO-1, and actin filaments.Cell structure and function · 2025Article
- Paths to stability - actin regulation of adherens junction mechanics.Journal of cell science · 2025Review
- Multi-level Force-dependent Allosteric Enhancement of αE-catenin Binding to F-actin by Vinculin.Journal of molecular biology · 2023Article
- Single-cell adhesivity distribution of glycocalyx digested cancer cells from high spatial resolution label-free biosensor measurements.Matrix biology plus · 2022Article
- Force-induced changes of α-catenin conformation stabilize vascular junctions independently of vinculin.Journal of cell science · 2021Article
- Plakophilin 3 and Par3 facilitate desmosomes' association with the apical junctional complex.Molecular biology of the cell · 2021Article
- Afadin regulates actomyosin organization through αE-catenin at adherens junctions.The Journal of cell biology · 2020Article
- Binding partner- and force-promoted changes in αE-catenin conformation probed by native cysteine labeling.Scientific reports · 2019Article
- Gut-liver axis signaling in portal hypertension.World journal of gastroenterology · 2019Review
- Article
- The adhesion modulation domain ofMolecular biology of the cell · 2019Article
- Mechanical stability of αT-catenin and its activation by force for vinculin binding.Molecular biology of the cell · 2019Article
- Morphologic determinant of tight junctions revealed by claudin-3 structures.Nature communications · 2019Article
- Oral Mucosal Epithelial Cells.Frontiers in immunology · 2019Review
- Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions.Nature communications · 2018Article
- Exclusion from spheroid formation identifies loss of essential cell-cell adhesion molecules in colon cancer cells.Scientific reports · 2018Article
- Salt bridges gate α-catenin activation at intercellular junctions.Molecular biology of the cell · 2018Article
- α-Catenin homodimers are recruited to phosphoinositide-activated membranes to promote adhesion.The Journal of cell biology · 2017Article
- Cell-cell adhesion in metazoans relies on evolutionarily conserved features of the α-catenin·β-catenin-binding interface.The Journal of biological chemistry · 2017Article
- Cadherin-mediated cell-cell interactions in normal and cancer cells.Tissue barriers · 2017Review
48 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction of cadherin-catenin complex with the actin-based cytoskeleton through alpha-catenin is indispensable for cadherin-based cell adhesion activity. We reported previously that E-cadherin-alpha-catenin fusion molecules showed cell adhesion and cytoskeleton binding activities when expressed in nonepithelial L cells. Here, we constructed deletion mutants of E-cadherin-alpha-catenin fusion molecules lacking various domains of alpha-catenin and introduced them into L cells. Detailed analysis identified three distinct functional domains of alpha-catenin: a vinculin/alpha-actinin-binding domain, a ZO-1-binding domain, and an adhesion-modulation domain. Furthermore, cell dissociation assay revealed that the fusion molecules containing the ZO-1-binding domain in addition to the adhesion-modulation domain conferred the strong state of cell adhesion activity on transfectants, although those lacking the ZO-1-binding domain conferred only the weak state. The disorganization of actin-based cytoskeleton by cytochalasin D treatment shifted the cadherin-based cell adhesion from the strong to the weak state. In the epithelial cells, where alpha-catenin was not precisely colocalized with ZO-1, the ZO-1-binding domain did not completely support the strong state of cell adhesion activity. Our studies showed that the interaction of alpha-catenin with the actin-based cytoskeleton through the ZO-1-binding domain is required for the strong state of E-cadherin-based cell adhesion activity.
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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.