ArticleFEBS letters2021
Crowding tunes the organization and mechanics of actin bundles formed by crosslinking proteins.
Article in FEBS letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The trial behind it
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- CaMKII generates actin bundle morphology and mechanics distinct from canonical bivalent cross-linkers.bioRxiv : the preprint server for biology · 2026Article
- Crosslinked F-actin networks regulate load-dependent energy conversion.Communications biology · 2026Article
- Underestimated role of macromolecular crowding in bioengineeredMaterials today. Bio · 2025Article
- Characterization, Enrichment, and Computational Modeling of Cross-Linked Actin Networks in Transformed Trabecular Meshwork Cells.Investigative ophthalmology & visual science · 2025Article
- Self-organized spatial targeting of contractile actomyosin rings for synthetic cell division.Nature communications · 2024Article
- Characterization, enrichment, and computational modeling of cross-linked actin networks in trabecular meshwork cells.bioRxiv : the preprint server for biology · 2024Article
- Fascin-1 in Cancer Cell Metastasis: Old Target-New Insights.International journal of molecular sciences · 2023Review
- Molecular Basis for Actin Polymerization Kinetics Modulated by Solution Crowding.Biomolecules · 2023Article
- Getting cells into shape by calcium-dependent actin cross-linking proteins.Frontiers in cell and developmental biology · 2023Review
- Regulation of Actin Bundle Mechanics and Structure by Intracellular Environmental Factors.Frontiers in physics · 2021Article
- Actin Bundle Nanomechanics and Organization Are Modulated by Macromolecular Crowding and Electrostatic Interactions.Frontiers in molecular biosciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Fascin and α-actinin form higher-ordered actin bundles that mediate numerous cellular processes including cell morphogenesis and movement. While it is understood crosslinked bundle formation occurs in crowded cytoplasm, how crowding affects the bundling activities of the two crosslinking proteins is not known. Here, we demonstrate how solution crowding modulates the organization and mechanical properties of fascin- and α-actinin-induced bundles, utilizing total internal reflection fluorescence and atomic force microscopy imaging. Molecular dynamics simulations support the inference that crowding reduces binding interaction between actin filaments and fascin or the calponin homology 1 domain of α-actinin evidenced by interaction energy and hydrogen bonding analysis. Based on our findings, we suggest a mechanism of crosslinked actin bundle assembly and mechanics in crowded intracellular environments.
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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.