ArticleNature communications2023
Molecular basis and cellular functions of vinculin-actin directional catch bonding.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Linking molecular tension and cellular tractions: a multiscale approach to focal adhesion mechanics.Communications biology · 2026Article
- Parallel in-register contact propensity predicts the Amyloidogenicity of ADan and ABri in familial dementias.International journal of biological macromolecules · 2026Article
- Shape, Strain, and Stability: Epithelia Under High Strain.bioRxiv : the preprint server for biology · 2025Article
- Built-In Electric Field Accelerates Nanotopography-Mediated Enhancement of Vascularized Osseointegration via CaSmall science · 2025Article
- 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
- Determinants for Substoichiometric Inhibition of IAPP and Aβ Amyloid Aggregations by Bri2 BRICHOS.ACS chemical neuroscience · 2025Article
- Molecular simulation approaches to probing the effects of mechanical forces in the actin cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Detection of fluorescent protein mechanical switching in cellulo.Cell reports methods · 2024Article
- Theory and Examples of Catch Bonds.The journal of physical chemistry. B · 2024Article
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6 authors.
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Abstract
The ability of cells and tissues to respond differentially to mechanical forces applied in distinct directions is mediated by the ability of load-bearing proteins to preferentially maintain physical linkages in certain directions. However, the molecular basis and biological consequences of directional force-sensitive binding remain unclear. Vinculin (Vcn) is a load-bearing linker protein that exhibits directional catch bonding due to interactions between the Vcn tail domain (Vt) and filamentous (F)-actin. We developed a computational approach to predict Vcn residues involved in directional catch bonding and produced a set of associated Vcn variants with unaltered Vt structure, actin binding, or phospholipid interactions. Incorporation of the variants did not affect Vcn activation but reduced Vcn loading and altered exchange dynamics, consistent with the loss of directional catch bonding. Expression of Vcn variants perturbed the coordination of subcellular structures and cell migration, establishing key cellular functions for Vcn directional catch bonding.
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