ArticleThe European physical journal. E, Soft matter2015
A single charge in the actin binding domain of fascin can independently tune the linear and non-linear response of an actin bundle network.
Article in The European physical journal. E, Soft matter, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 18 citations in OpenAlex.
- The role of linker length and composition in actin binding and bundling by palladin.The Biochemical journal · 2026Article
- The Role of Linker Length and Composition in Actin Binding and Bundling by Palladin.bioRxiv : the preprint server for biology · 2025Article
- Topological defects produce kinks in biopolymer filament bundles.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Actin binding proteins (ABPs) not only set the structure of actin filament assemblies but also mediate the frequency-dependent viscoelastic moduli of cross-linked and bundled actin networks. Point mutations in the actin binding domain of those ABPs can tune the association and dissociation dynamics of the actin/ABP bond and thus modulate the network mechanics both in the linear and non-linear response regime. We here demonstrate how the exchange of a single charged amino acid in the actin binding domain of the ABP fascin triggers such a modulation of the network rheology. Whereas the overall structure of the bundle networks is conserved, the transition point from strain-hardening to strain-weakening sensitively depends on the cross-linker off-rate and the applied shear rate. Our experimental results are consistent both with numerical simulations of a cross-linked bundle network and a theoretical description of the bundle network mechanics which is based on non-affine bending deformations and force-dependent cross-link dynamics.
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