ArticleCell adhesion & migration
Vinculin regulation of F-actin bundle formation: what does it mean for the cell?
Article in Cell adhesion & migration. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Direct Arp2/3-vinculin binding is required for pseudopod extension, but only on compliant substrates and in 3D.iScience · 2025Article
- Rbfox1 controls alternative splicing of focal adhesion genes in cardiac muscle cells.Journal of molecular cell biology · 2024Article
- Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024Article
- Mesenchymal stem cells lose the senescent phenotype under 3D cultivation.Stem cell research & therapy · 2023Article
- Reversible rearrangement of the cellular cytoskeleton: A key to the broad-spectrum antiviral activity of novel amphiphilic polymers.Materials today. Bio · 2023Article
- Article
- The effect of allyl isothiocyanate on chondrocyte phenotype is matrix stiffness-dependent: Possible involvement of TRPA1 activation.Frontiers in molecular biosciences · 2023Article
- Analysis of Actin and Focal Adhesion Organisation in U2OS Cells on Polymer Nanostructures.Nanoscale research letters · 2021Article
- Ultra-Thin Porous PDLLA Films Promote Generation, Maintenance, and Viability of Stem Cell Spheroids.Frontiers in bioengineering and biotechnology · 2021Article
- Distinct Binding Modes of Vinculin Isoforms Underlie Their Functional Differences.Structure (London, England : 1993) · 2019Article
- Vinculin in cell-cell and cell-matrix adhesions.Cellular and molecular life sciences : CMLS · 2017Review
- Targeted Proteomics-Driven Computational Modeling of Macrophage S1P Chemosensing.Molecular & cellular proteomics : MCP · 2015Article
- Vinculin network-mediated cytoskeletal remodeling regulates contractile function in the aging heart.Science translational medicine · 2015Article
- Lipid binding promotes oligomerization and focal adhesion activity of vinculin.The Journal of cell biology · 2014Article
- Phosphorylation at Y1065 in vinculin mediates actin bundling, cell spreading, and mechanical responses to force.Biochemistry · 2014Article
- Mechanisms of neuronal membrane sealing following mechanical trauma.Neuroscience bulletin · 2014Review
- Article
- A helping hand: How vinculin contributes to cell-matrix and cell-cell force transfer.Cell adhesion & migration · 2014Article
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3 authors at 2 institutions in 1 country.
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Abstract
Vinculin is an essential cell adhesion protein, found at both focal adhesions and adherens junctions, where it couples transmembrane proteins to the actin cytoskeleton. Vinculin is involved in controlling cell shape, motility and cell survival, and has more recently been shown to play a role in force transduction. The tail domain of vinculin (Vt) has the ability to both bind and bundle actin filaments. Binding to actin induces a conformational change in Vt believed to promote formation of a Vt dimer that is able to crosslink actin filaments. We have recently provided additional evidence for the actin-induced Vt dimer and have shown that the vinculin carboxyl (C)-terminal hairpin is critical for both the formation of the Vt dimer and for bundling F-actin. We have also demonstrated the importance of the C-terminal hairpin in cells as deletion of this region impacts both adhesion properties and force transduction. Intriguingly, we have identified bundling deficient variants of vinculin that show different cellular phenotypes. These results suggest additional role(s) for the C-terminal hairpin, distinct from its bundling function. In this commentary, we will expand on our previous findings and further investigate these actin bundling deficient vinculin variants.
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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.