ArticleThe Journal of cell biology1997
Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 442 papers.
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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
442 citing papers in PubMed, 1,050 citations in OpenAlex.
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- Mechanisms of disassembly at the actin filament pointed and barbed ends.Science advances · 2026Article
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- Structural Biology of Actin: Interplay Between Molecular Assembly, Conformational Polymorphism and ATPase.Sub-cellular biochemistry · 2026Review
- Molecular dissection of actin depolymerizing factors in wheat and its progenitors: their dynamic expression under elevated temperature stress.Molecular biology reports · 2025Article
- Neuronal Actin Remodeling and Its Role in Higher Nervous Activity.International journal of molecular sciences · 2025Review
- Structure and Functions of Actin and Actin-Binding Proteins inPathogens (Basel, Switzerland) · 2025Review
- Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.Cytoskeleton (Hoboken, N.J.) · 2025Article
- A generalized theoretical framework to investigate multicomponent actin dynamics.PLoS computational biology · 2025Article
- Optogenetic actin network assembly on lipid bilayer uncovers the network density-dependent functions of actin-binding proteins.Nature communications · 2025Article
- Role of Tpm Isoforms Produced by theBiomolecules · 2025Article
- Microscopic and structural observations of actin filament capping and severing by cytochalasin D.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular Dynamics of Trogocytosis and Other Contact-Dependent Cell Trafficking Mechanisms in Tumor Pathogenesis.Cancers · 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
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Reducing Cofilin dosage makes embryos resilient to heat stress.bioRxiv : the preprint server for biology · 2025Article
- Role of the cytoskeleton in cellular reprogramming: effects of biophysical and biochemical factors.Frontiers in molecular biosciences · 2025Review
- The open to closed D-loop conformational switch determines length in filopodia-like actin bundles.The Biochemical journal · 2024Article
- Article
- Beyond Glycolysis: Aldolase A Is a Novel Effector in Reelin-Mediated Dendritic Development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
382 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin-binding proteins of the actin depolymerizing factor (ADF)/cofilin family are thought to control actin-based motile processes. ADF1 from Arabidopsis thaliana appears to be a good model that is functionally similar to other members of the family. The function of ADF in actin dynamics has been examined using a combination of physical-chemical methods and actin-based motility assays, under physiological ionic conditions and at pH 7.8. ADF binds the ADP-bound forms of G- or F-actin with an affinity two orders of magnitude higher than the ATP- or ADP-Pi-bound forms. A major property of ADF is its ability to enhance the in vitro turnover rate (treadmilling) of actin filaments to a value comparable to that observed in vivo in motile lamellipodia. ADF increases the rate of propulsion of Listeria monocytogenes in highly diluted, ADF-limited platelet extracts and shortens the actin tails. These effects are mediated by the participation of ADF in actin filament assembly, which results in a change in the kinetic parameters at the two ends of the actin filament. The kinetic effects of ADF are end specific and cannot be accounted for by filament severing. The main functionally relevant effect is a 25-fold increase in the rate of actin dissociation from the pointed ends, while the rate of dissociation from the barbed ends is unchanged. This large increase in the rate-limiting step of the monomer-polymer cycle at steady state is responsible for the increase in the rate of actin-based motile processes. In conclusion, the function of ADF is not to sequester G-actin. ADF uses ATP hydrolysis in actin assembly to enhance filament dynamics.
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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.