ArticlePLoS biology2011
Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin.
Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.
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116 citing papers in PubMed, 168 citations in OpenAlex.
- Physical confinement modulates the rate-limiting transition in the release of phosphate from actin filaments.Science advances · 2026Article
- Inorganic phosphate rapidly switches the stability of Arp2/3-induced actin branches.The Journal of cell biology · 2026Article
- Rapid actin filament turnover maintains cortical connectivity while allowing for cell cortex deformation and flow.bioRxiv : the preprint server for biology · 2026Article
- Physical Confinement Modulates the Rate-Limiting Transition in the Release of Phosphate from Actin Filaments.bioRxiv : the preprint server for biology · 2026Article
- Structural Biology of Actin: Interplay Between Molecular Assembly, Conformational Polymorphism and ATPase.Sub-cellular biochemistry · 2026Review
- ATP-dependent actin barbed-end fluctuations at steady state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A generalized theoretical framework to investigate multicomponent actin dynamics.PLoS computational biology · 2025Article
- Hydrolysis-dependent severing tunes internal monomeric heterogeneity to shape actin length distributions.bioRxiv : the preprint server for biology · 2025Article
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- 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
- Histidine 73 methylation coordinates β-actin plasticity in response to key environmental factors.Nature communications · 2025Article
- Sequential recruitment of F-BAR proteins controls cytoskeletal crosstalk at the yeast bud neck.Current biology : CB · 2025Article
- Polymer dynamics of Alp7A reveals how two critical concentrations govern assembly of dynamically unstable actin-like proteins.Molecular biology of the cell · 2024Article
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Mechanism of phosphate release from actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Fascin-induced bundling protects actin filaments from disassembly by cofilin.The Journal of cell biology · 2024Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.European journal of cell biology · 2024Article
- Mechanism of Phosphate Release from Actin Filaments.bioRxiv : the preprint server for biology · 2024Article
- Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament.Nature structural & molecular biology · 2024Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.bioRxiv : the preprint server for biology · 2024Article
56 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hydrolysis of ATP associated with actin and profilin-actin polymerization is pivotal in cell motility. It is at the origin of treadmilling of actin filaments and controls their dynamics and mechanical properties, as well as their interactions with regulatory proteins. The slow release of inorganic phosphate (Pi) that follows rapid cleavage of ATP gamma phosphate is linked to an increase in the rate of filament disassembly. The mechanism of Pi release in actin filaments has remained elusive for over 20 years. Here, we developed a microfluidic setup to accurately monitor the depolymerization of individual filaments and determine their local ADP-Pi content. We demonstrate that Pi release in the filament is not a vectorial but a random process with a half-time of 102 seconds, irrespective of whether the filament is assembled from actin or profilin-actin. Pi release from the depolymerizing barbed end is faster (half-time of 0.39 seconds) and further accelerated by profilin. Profilin accelerates the depolymerization of both ADP- and ADP-Pi-F-actin. Altogether, our data show that during elongation from profilin-actin, the dissociation of profilin from the growing barbed end is not coupled to Pi release or to ATP cleavage on the terminal subunit. These results emphasize the potential of microfluidics in elucidating actin regulation at the scale of individual filaments.
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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.