ArticleeLife2022
The molecular mechanism of load adaptation by branched actin networks.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 40 citations in OpenAlex.
- Actin-membrane interface stress regulates Arp2/3-branched actin density during lamellipodial protrusion.bioRxiv : the preprint server for biology · 2026Article
- Class-I myosin responds to changes in membrane tension during clathrin-mediated endocytosis in human induced pluripotent stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cold atmospheric plasma promotes migration persistence, through induced HBiophysical journal · 2026Article
- Tissue fluidity mediates a trade-off between the speed and accuracy of multicellular patterning by cell sorting.Biophysical journal · 2025Article
- Actin cytoskeleton protection by the formin-mediated safety valve.Current opinion in cell biology · 2025Review
- Myosins 1e/f at the podosome base regulate podosome dynamics and promote macrophage migration.European journal of cell biology · 2025Article
- Adherent cells sustain membrane tension gradients independently of migration.Nature communications · 2025Article
- Actin filament assembly driven by distributive polymerases clustered on membrane surfaces.bioRxiv : the preprint server for biology · 2025Article
- The mechanism of dynamic steady states in lamellipodia.PLoS computational biology · 2025Article
- Tissue Fluidity Mediates a Trade-off Between the Speed and Accuracy of Multicellular Patterning by Cell Sorting.bioRxiv : the preprint server for biology · 2025Article
- Cell condensation initiates organogenesis: the role of actin dynamics in supracellular self-organizing process.Cell & bioscience · 2025Review
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Article
- Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks.The Journal of biological chemistry · 2025Article
- Energy-based modelling of single actin filament polymerization using bond graphs.Journal of the Royal Society, Interface · 2025Article
- Myosin-I synergizes with Arp2/3 complex to enhance the pushing forces of branched actin networks.Science advances · 2024Article
- Designed Ankyrin Repeat Proteins as Actin Labels of Distinct Cytoskeletal Structures in Living Cells.ACS nano · 2024Article
- Adaptive nonequilibrium design of actin-based metamaterials: Fundamental and practical limits of control.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Myosin-I Synergizes with Arp2/3 Complex to Enhance Pushing Forces of Branched Actin Networks.bioRxiv : the preprint server for biology · 2024Article
- Regeneration of actin filament branches from the same Arp2/3 complex.Science advances · 2024Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Branched actin networks are self-assembling molecular motors that move biological membranes and drive many important cellular processes, including phagocytosis, endocytosis, and pseudopod protrusion. When confronted with opposing forces, the growth rate of these networks slows and their density increases, but the stoichiometry of key components does not change. The molecular mechanisms governing this force response are not well understood, so we used single-molecule imaging and AFM cantilever deflection to measure how applied forces affect each step in branched actin network assembly. Although load forces are observed to increase the density of growing filaments, we find that they actually decrease the rate of filament nucleation due to inhibitory interactions between actin filament ends and nucleation promoting factors. The force-induced increase in network density turns out to result from an exponential drop in the rate constant that governs filament capping. The force dependence of filament capping matches that of filament elongation and can be explained by expanding Brownian Ratchet theory to cover both processes. We tested a key prediction of this expanded theory by measuring the force-dependent activity of engineered capping protein variants and found that increasing the size of the capping protein increases its sensitivity to applied forces. In summary, we find that Brownian Ratchets underlie not only the ability of growing actin filaments to generate force but also the ability of branched actin networks to adapt their architecture to changing loads.
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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.