ArticlePLoS computational biology2013
The interaction of vinculin with actin.
Article in PLoS computational biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 59 citations in OpenAlex.
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- A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS.Protein science : a publication of the Protein Society · 2025Article
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- Principles and regulation of mechanosensing.Journal of cell science · 2024Review
- Advances in modeling cellular mechanical perceptions and responses via the membrane-cytoskeleton-nucleus machinery.Mechanobiology in medicine · 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
- Vinculin Y822 is an important determinant of ligand binding.Journal of cell science · 2023Article
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- Complete Model of Vinculin Suggests the Mechanism of Activation by Helical Super-Bundle Unfurling.The protein journal · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vinculin can interact with F-actin both in recruitment of actin filaments to the growing focal adhesions and also in capping of actin filaments to regulate actin dynamics. Using molecular dynamics, both interactions are simulated using different vinculin conformations. Vinculin is simulated either with only its vinculin tail domain (Vt), with all residues in its closed conformation, with all residues in an open I conformation, and with all residues in an open II conformation. The open I conformation results from movement of domain 1 away from Vt; the open II conformation results from complete dissociation of Vt from the vinculin head domains. Simulation of vinculin binding along the actin filament showed that Vt alone can bind along the actin filaments, that vinculin in its closed conformation cannot bind along the actin filaments, and that vinculin in its open I conformation can bind along the actin filaments. The simulations confirm that movement of domain 1 away from Vt in formation of vinculin 1 is sufficient for allowing Vt to bind along the actin filament. Simulation of Vt capping actin filaments probe six possible bound structures and suggest that vinculin would cap actin filaments by interacting with both S1 and S3 of the barbed-end, using the surface of Vt normally occluded by D4 and nearby vinculin head domain residues. Simulation of D4 separation from Vt after D1 separation formed the open II conformation. Binding of open II vinculin to the barbed-end suggests this conformation allows for vinculin capping. Three binding sites on F-actin are suggested as regions that could link to vinculin. Vinculin is suggested to function as a variable switch at the focal adhesions. The conformation of vinculin and the precise F-actin binding conformation is dependent on the level of mechanical load on the focal adhesion.
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