ArticleThe Journal of biological chemistry2010
Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 76 citations in OpenAlex.
- Actomyosin-dependent assembly of the mechanosensitive machinery from adherens junctions triggers actin polymerization and organization.Science advances · 2026Article
- Genetically engineered ESC-derived embryos reveal Vinculin-dependent force responses required for mammalian neural tube closure.bioRxiv : the preprint server for biology · 2025Article
- Activation of dimerized BRS3-EP3 suppresses melanoma cell migration through coupling GαFundamental research · 2025Article
- The mechanical response of vinculin.Science advances · 2025Article
- Vinculin-Arp2/3 interaction inhibits branched actin assembly to control migration and proliferation.Life science alliance · 2025Article
- Proteomic signatures of retinal pigment epithelium-derived exosomes in myopic and non-myopic tree shrew eyes.Frontiers in medicine · 2025Article
- Talin and vinculin combine their activities to trigger actin assembly.Nature communications · 2024Article
- Matrix stiffening promotes perinuclear clustering of mitochondria.Molecular biology of the cell · 2024Article
- Multi-omics analysis to reveal the synergistic mechanism underlying the multiple ingredients ofFrontiers in pharmacology · 2024Article
- Shared and Unique Disease Pathways in Amyotrophic Lateral Sclerosis and Parkinson's Disease Unveiled in Peripheral Blood Mononuclear Cells.ACS chemical neuroscience · 2023Article
- To investigate the mechanism of Yiwei Decoction in the treatment of premature ovarian insufficiency-related osteoporosis using transcriptomics, network pharmacology and molecular docking techniques.Scientific reports · 2023Article
- Development of a Prediction Model for Short-Term Remission of Patients with Crohn's Disease Treated with Anti-TNF Drugs.International journal of molecular sciences · 2023Article
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- Mechanical Properties of Colorectal Cancer Cells Determined by Dynamic Atomic Force Microscopy: A Novel Biomarker.Cancers · 2022Article
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- Analysis of Actin and Focal Adhesion Organisation in U2OS Cells on Polymer Nanostructures.Nanoscale research letters · 2021Article
- Comprehensive Proteomic Analysis of Colon Cancer Tissue Revealed the Reason for the Worse Prognosis of Right-Sided Colon Cancer and Mucinous Colon Cancer at the Protein Level.Current oncology (Toronto, Ont.) · 2021Article
- CHIP-dependent regulation of the actin cytoskeleton is linked to neuronal cell membrane integrity.iScience · 2021Article
- Vinculin-mediated axon growth requires interaction with actin but not talin in mouse neocortical neurons.Cellular and molecular life sciences : CMLS · 2021Article
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Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The focal adhesion protein vinculin is an actin-binding protein involved in the mechanical coupling between the actin cytoskeleton and the extracellular matrix. An autoinhibitory interaction between the N-terminal head (Vh) and the C-terminal tail (Vt) of vinculin masks an actin filament side-binding domain in Vt. The binding of several proteins to Vh disrupts this intramolecular interaction and exposes the actin filament side-binding domain. Here, by combining kinetic assays and microscopy observations, we show that Vt inhibits actin polymerization by blocking the barbed ends of actin filaments. In low salt conditions, Vt nucleates actin filaments capped at their barbed ends. We determined that the interaction between vinculin and the barbed end is characterized by slow association and dissociation rate constants. This barbed end capping activity requires C-terminal amino acids of Vt that are dispensable for actin filament side binding. Like the side-binding domain, the capping domain of vinculin is masked by an autoinhibitory interaction between Vh and Vt. In contrast to the side-binding domain, the capping domain is not unmasked by the binding of a talin domain to Vh and requires the dissociation of an additional autoinhibitory interaction. Finally, we show that vinculin and the formin mDia1, which is involved in the processive elongation of actin filaments in focal adhesions, compete for actin filament barbed ends.
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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.