ArticleBiophysical journal2020
Different Vinculin Binding Sites Use the Same Mechanism to Regulate Directional Force Transduction.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Review
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- Sarcoglycans Role in Actin Cytoskeleton Dynamics and Cell Adhesion of Human Articular Chondrocytes: New Insights from siRNA-Mediated Gene Silencing.International journal of molecular sciences · 2025Article
- IpaA reveals distinct modes of vinculin activation duringLife science alliance · 2024Article
- Extracellular Matrix Cues Regulate Mechanosensing and Mechanotransduction of Cancer Cells.Cells · 2024Review
- Allosteric activation of vinculin by talin.Nature communications · 2023Article
- An ensemble of cadherin-catenin-vinculin complex employs vinculin as the major F-actin binding mode.Biophysical journal · 2023Article
- Remodeling of the focal adhesion complex by hydrogen-peroxide-induced senescence.Scientific reports · 2023Article
- Unravelling cell migration: defining movement from the cell surface.Cell adhesion & migration · 2022Review
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- Review
- From the Matrix to the Nucleus and Back: Mechanobiology in the Light of Health, Pathologies, and Regeneration of Oral Periodontal Tissues.Biomolecules · 2021Review
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- Mechanical Unfolding of Proteins-A Comparative Nonequilibrium Molecular Dynamics Study.Biophysical journal · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vinculin is a universal adaptor protein that transiently reinforces the mechanical stability of adhesion complexes. It stabilizes mechanical connections that cells establish between the actomyosin cytoskeleton and the extracellular matrix via integrins or to neighboring cells via cadherins, yet little is known regarding its mechanical design. Vinculin binding sites (VBSs) from different nonhomologous actin-binding proteins use conserved helical motifs to associate with the vinculin head domain. We studied the mechanical stability of such complexes by pulling VBS peptides derived from talin, α-actinin, and Shigella IpaA out of the vinculin head domain. Experimental data from atomic force microscopy single-molecule force spectroscopy and steered molecular dynamics (SMD) simulations both revealed greater mechanical stability of the complex for shear-like than for zipper-like pulling configurations. This suggests that reinforcement occurs along preferential force directions, thus stabilizing those cytoskeletal filament architectures that result in shear-like pulling geometries. Large force-induced conformational changes in the vinculin head domain, as well as protein-specific fine-tuning of the VBS sequence, including sequence inversion, allow for an even more nuanced force response.
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