ArticleeLife2019
Profilin and formin constitute a pacemaker system for robust actin filament growth.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
What it found
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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
69 citing papers in PubMed.
- Profilin promotes lamellipodium protrusion by tuning the antagonistic activities of capping protein and VASP.Nature communications · 2026Article
- Rapid actin filament turnover maintains cortical connectivity while allowing for cell cortex deformation and flow.bioRxiv : the preprint server for biology · 2026Article
- AAV2 Crosslinks Actin Filaments: Implications for AAV Gene Therapy Vector Design.bioRxiv : the preprint server for biology · 2026Article
- Asymmetric distribution of actin-related proteins in the earlybioRxiv : the preprint server for biology · 2026Article
- Cooperative and divergent properties of bacterial actin isoforms inBiophysics and physicobiology · 2026Article
- Global Research Trends and Hotspots in Cardiac Devices: A Bibliometric and Visual Analysis.Healthcare (Basel, Switzerland) · 2025Review
- Actin cytoskeleton protection by the formin-mediated safety valve.Current opinion in cell biology · 2025Review
- Actin filament assembly driven by distributive polymerases clustered on membrane surfaces.bioRxiv : the preprint server for biology · 2025Article
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Modulation of host ATP levels by secreted bacterial effectors.Nature communications · 2025Article
- Twinfilin is a nonprocessive depolymerase which synergizes with formin to dramatically accelerate actin filament uncapping by 300-fold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Membrane-associated polymerases deliver most of the actin subunits to a lamellipodial network.bioRxiv : the preprint server for biology · 2025Article
- Using ALS to understand profilin 1's diverse roles in cellular physiology.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Control of plasma membrane-associated actin polymerization specifies the pattern of the cell wall in xylem vessels.Nature communications · 2025Article
- The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Biochemical characterization of cardiac α-actin mutations A21V and D26N implicated in hypertrophic cardiomyopathy.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Talin and vinculin combine their activities to trigger actin assembly.Nature communications · 2024Article
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Phalloidin and DNase I-bound F-actin pointed end structures reveal principles of filament stabilization and disassembly.Nature communications · 2024Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
The actin cytoskeleton drives many essential biological processes, from cell morphogenesis to motility. Assembly of functional actin networks requires control over the speed at which actin filaments grow. How this can be achieved at the high and variable levels of soluble actin subunits found in cells is unclear. Here we reconstitute assembly of mammalian, non-muscle actin filaments from physiological concentrations of profilin-actin. We discover that under these conditions, filament growth is limited by profilin dissociating from the filament end and the speed of elongation becomes insensitive to the concentration of soluble subunits. Profilin release can be directly promoted by formin actin polymerases even at saturating profilin-actin concentrations. We demonstrate that mammalian cells indeed operate at the limit to actin filament growth imposed by profilin and formins. Our results reveal how synergy between profilin and formins generates robust filament growth rates that are resilient to changes in the soluble subunit concentration.
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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.