ArticleMolecular and cellular biology2005
Structural dynamics of alpha-actinin-vinculin interactions.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 49 papers.
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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.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
49 citing papers in PubMed, 97 citations in OpenAlex.
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- Multi-domain interaction mediated strength-building in human α-actinin dimers unveiled by direct single-molecule quantification.Nature communications · 2024Article
- Alternative molecular mechanisms for force transmission at adherens junctions via β-catenin-vinculin interaction.Nature communications · 2024Article
- The mechanical cell - the role of force dependencies in synchronising protein interaction networks.Journal of cell science · 2022Review
- Synaptopodin stress fiber and contractomere at the epithelial junction.The Journal of cell biology · 2022Article
- Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022Review
- Severe pantothenic acid deficiency induces alterations in the intestinal mucosal proteome of starter Pekin ducks.BMC genomics · 2021Article
- DCBLD1 is associated with the integrin signaling pathway and has prognostic value in non-small cell lung and invasive breast carcinoma.Scientific reports · 2021Article
- The Cryogenic Electron Microscopy Structure of the Cell Adhesion Regulator Metavinculin Reveals an Isoform-Specific Kinked Helix in Its Cytoskeleton Binding Domain.International journal of molecular sciences · 2021Article
- Article
- A distinct talin2 structure directs isoform specificity in cell adhesion.The Journal of biological chemistry · 2020Article
- Different Vinculin Binding Sites Use the Same Mechanism to Regulate Directional Force Transduction.Biophysical journal · 2020Article
- Phagocytic Integrins: Activation and Signaling.Frontiers in immunology · 2020Review
- Computational and experimental analysis of bioactive peptide linear motifs in the integrin adhesome.PloS one · 2019Article
- The interaction of talin with the cell membrane is essential for integrin activation and focal adhesion formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Myosin-1c promotes E-cadherin tension and force-dependent recruitment of α-actinin to the epithelial cell junction.Journal of cell science · 2018Article
- Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Dynamic Regulation of α-Actinin's Calponin Homology Domains on F-Actin.Biophysical journal · 2016Article
- Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturation.The Journal of cell biology · 2015Article
Corrections and comments
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- Erratum issued
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Alpha-actinin and vinculin orchestrate reorganization of the actin cytoskeleton following the formation of adhesion junctions. alpha-Actinin interacts with vinculin through the binding of an alpha-helix (alphaVBS) present within the R4 spectrin repeat of its central rod domain to vinculin's N-terminal seven-helical bundle domain (Vh1). The Vh1:alphaVBS structure suggests that alphaVBS first unravels from its buried location in the triple-helical R4 repeat to allow it to bind to vinculin. alphaVBS binding then induces novel conformational changes in the N-terminal helical bundle of Vh1, which disrupt its intramolecular association with vinculin's tail domain and which differ from the alterations in Vh1 provoked by the binding of talin. Surprisingly, alphaVBS binds to Vh1 in an inverted orientation compared to the binding of talin's VBSs to vinculin. Importantly, the binding of alphaVBS and talin's VBSs to vinculin's Vh1 domain appear to also trigger distinct conformational changes in full-length vinculin, opening up distant regions that are buried in the inactive molecule. The data suggest a model where vinculin's Vh1 domain acts as a molecular switch that undergoes distinct structural changes provoked by talin and alpha-actinin binding in focal adhesions versus adherens junctions, respectively.
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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.