ArticleNature communications2022
F-actin architecture determines constraints on myosin thick filament motion.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 55 citations in OpenAlex.
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- A multicellular star-shaped actin network underpins epithelial organization and connectivity.Nature communications · 2025Article
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- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Cell signaling facilitates apical constriction by basolaterally recruiting Arp2/3 via Rac and WAVE.The Journal of cell biology · 2025Article
- Nucleating amoeboid cancer cell motility with Diaphanous related formins.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Vinculin-Arp2/3 interaction inhibits branched actin assembly to control migration and proliferation.Life science alliance · 2025Article
- Direct detection of deformation modes on varying length scales in active biopolymer networks.bioRxiv : the preprint server for biology · 2025Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Active stresses are generated and transmitted throughout diverse F-actin architectures within the cell cytoskeleton, and drive essential behaviors of the cell, from cell division to migration. However, while the impact of F-actin architecture on the transmission of stress is well studied, the role of architecture on the ab initio generation of stresses remains less understood. Here, we assemble F-actin networks in vitro, whose architectures are varied from branched to bundled through F-actin nucleation via Arp2/3 and the formin mDia1. Within these architectures, we track the motions of embedded myosin thick filaments and connect them to the extent of F-actin network deformation. While mDia1-nucleated networks facilitate the accumulation of stress and drive contractility through enhanced actomyosin sliding, branched networks prevent stress accumulation through the inhibited processivity of thick filaments. The reduction in processivity is due to a decrease in translational and rotational motions constrained by the local density and geometry of F-actin.
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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.