ArticleThe Journal of biological chemistry2015
Structural Determinants of the Mechanical Stability of α-Catenin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- 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
- Single-molecule force spectroscopy reveals intra- and intermolecular interactions ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- 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
- 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
- The α-Catenin mechanosensing M region is required for cell adhesion during tissue morphogenesis.The Journal of cell biology · 2023Article
- C. elegans srGAP is an α-catenin M domain-binding protein that strengthens cadherin-dependent adhesion during morphogenesis.Development (Cambridge, England) · 2022Article
- Appropriate tension sensitivity of α-catenin ensures rounding morphogenesis of epithelial spheroids.Cell structure and function · 2022Article
- Article
- Different Vinculin Binding Sites Use the Same Mechanism to Regulate Directional Force Transduction.Biophysical journal · 2020Article
- Binding partner- and force-promoted changes in αE-catenin conformation probed by native cysteine labeling.Scientific reports · 2019Article
- Mechanical stability of αT-catenin and its activation by force for vinculin binding.Molecular biology of the cell · 2019Article
- Unraveling the mechanism of the cadherin-catenin-actin catch bond.PLoS computational biology · 2018Article
- Real-time TIRF observation of vinculin recruitment to stretched α-catenin by AFM.Scientific reports · 2018Article
- Salt bridges gate α-catenin activation at intercellular junctions.Molecular biology of the cell · 2018Article
- Structural and functional characterization ofThe Journal of biological chemistry · 2017Article
- αT-Catenin Is a Constitutive Actin-binding α-Catenin That Directly Couples the Cadherin·Catenin Complex to Actin Filaments.The Journal of biological chemistry · 2016Article
- Mechano-adaptive sensory mechanism of α-catenin under tension.Scientific reports · 2016Article
- Distinct intramolecular interactions regulate autoinhibition of vinculin binding in αT-catenin and αE-catenin.The Journal of biological chemistryArticle
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
α-Catenin plays a crucial role in cadherin-mediated adhesion by binding to β-catenin, F-actin, and vinculin, and its dysfunction is linked to a variety of cancers and developmental disorders. As a mechanotransducer in the cadherin complex at intercellular adhesions, mechanical and force-sensing properties of α-catenin are critical to its proper function. Biochemical data suggest that α-catenin adopts an autoinhibitory conformation, in the absence of junctional tension, and biophysical studies have shown that α-catenin is activated in a tension-dependent manner that in turn results in the recruitment of vinculin to strengthen the cadherin complex/F-actin linkage. However, the molecular switch mechanism from autoinhibited to the activated state remains unknown for α-catenin. Here, based on the results of an aggregate of 3 μs of molecular dynamics simulations, we have identified a dynamic salt-bridge network within the core M region of α-catenin that may be the structural determinant of the stability of the autoinhibitory conformation. According to our constant-force steered molecular dynamics simulations, the reorientation of the MII/MIII subdomains under force may constitute an initial step along the transition pathway. The simulations also suggest that the vinculin-binding domain (subdomain MI) is intrinsically much less stable than the other two subdomains in the M region (MII and MIII). Our findings reveal several key insights toward a complete understanding of the multistaged, force-induced conformational transition of α-catenin to the activated conformation.
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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.