ArticleThe EMBO journal2007
Vinculin binding in its closed conformation by a helix addition mechanism.
Article in The EMBO journal, 2007. 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 32 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.
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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
32 citing papers in PubMed, 54 citations in OpenAlex.
- IpaA reveals distinct modes of vinculin activation duringLife science alliance · 2024Article
- Functional comparison of full-length palladin to isolated actin binding domain.Protein science : a publication of the Protein Society · 2023Article
- The Actin Network Interfacing Diverse Integrin-Mediated Adhesions.Biomolecules · 2023Review
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- 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
- A distinct talin2 structure directs isoform specificity in cell adhesion.The Journal of biological chemistry · 2020Article
- 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
- Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes.Journal of cell science · 2016Article
- Regulation of Intracellular Structural Tension by Talin in the Axon Growth and Regeneration.Molecular neurobiology · 2016Article
- Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Vinculin Interacts with the Chlamydia Effector TarP Via a Tripartite Vinculin Binding Domain to Mediate Actin Recruitment and Assembly at the Plasma Membrane.Frontiers in cellular and infection microbiology · 2015Article
- Review
- The interaction of vinculin with actin.PLoS computational biology · 2013Article
- αE-catenin is an autoinhibited molecule that coactivates vinculin.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The cytoskeletal protein α-catenin unfurls upon binding to vinculin.The Journal of biological chemistry · 2012Article
- Designing photoswitchable peptides using the AsLOV2 domain.Chemistry & biology · 2012Article
- Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin.Protein science : a publication of the Protein Society · 2012Article
- α-Catenin uses a novel mechanism to activate vinculin.The Journal of biological chemistry · 2012Article
- Vinculin motion modes analysis with elastic network model.International journal of molecular sciences · 2012Article
- The rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin.The Journal of biological chemistry · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Vinculin links integrin receptors to the actin cytoskeleton by binding to talin. Vinculin is held in an inactive, closed-clamp conformation through hydrophobic interactions between its head and tail domains, and vinculin activation has long been thought to be dependent upon severing the head-tail interaction. Talin, alpha-actinin, and the invasin IpaA of Shigella flexneri sever vinculin's head-tail interaction by inserting an alpha-helix into vinculin's N-terminal four-helical bundle, provoking extensive conformational changes by a helical bundle conversion mechanism; these alterations in vinculin structure displace its tail domain, allowing vinculin to bind to its other partners. IpaA harbors two juxtaposed alpha-helical vinculin-binding sites (VBS) in its C-terminus. Here, we report that the lower affinity VBS of IpaA can also bind to the adjacent C-terminal four-helical bundle of vinculin's head domain through a helix addition mechanism. These hydrophobic interactions do not alter the conformation of this helical bundle, and the architecture of the complex suggests that IpaA can simultaneously interact with both of the four-helical bundle domains of vinculin's N-terminus to stabilize vinculin-IpaA interactions.
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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.