ArticleThe Journal of cell biology2001
Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits.
Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 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
116 citing papers in PubMed, 250 citations in OpenAlex.
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Article
- Myosin-induced F-actin fragmentation facilitates contraction of actin networks.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Fascin-induced bundling protects actin filaments from disassembly by cofilin.The Journal of cell biology · 2024Article
- Deciphering the Cofilin Oligomers via Intermolecular Disulfide Bond Formation: A Coarse-Grained Molecular Dynamics Approach to Understanding Cofilin's Regulation on Actin Filaments.The journal of physical chemistry. B · 2024Article
- Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.Life science alliance · 2023Article
- Contribution of mechanical homeostasis to epithelial-mesenchymal transition.Cellular oncology (Dordrecht, Netherlands) · 2022Review
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Visualising the cytoskeletal machinery in neuronal growth cones using cryo-electron tomography.Journal of cell science · 2022Article
- Molecular and structural basis of actin filament severing by ADF/cofilin.Computational and structural biotechnology journal · 2022Article
- Review
- Long-Range and Directional Allostery of Actin Filaments Plays Important Roles in Various Cellular Activities.International journal of molecular sciences · 2020Review
- Directional allosteric regulation of protein filament length.Physical review. E · 2020Article
- Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Single-molecule nanopore sensing of actin dynamics and drug binding.Chemical science · 2019Article
- Coronin 1A depletion restores the nuclear stability and viability of Aip1/Wdr1-deficient neutrophils.The Journal of cell biology · 2019Article
- K336I mutant actin alters the structure of neighbouring protomers in filaments and reduces affinity for actin-binding proteins.Scientific reports · 2019Article
- Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Quantitative Variations with pH of Actin Depolymerizing Factor/Cofilin's Multiple Actions on Actin Filaments.Biochemistry · 2019Article
- The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments.The Journal of biological chemistry · 2018Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Proteins in the actin depolymerizing factor (ADF)/cofilin family are essential for rapid F-actin turnover, and most depolymerize actin in a pH-dependent manner. Complexes of human and plant ADF with F-actin at different pH were examined using electron microscopy and a novel method of image analysis for helical filaments. Although ADF changes the mean twist of actin, we show that it does this by stabilizing a preexisting F-actin angular conformation. In addition, ADF induces a large ( approximately 12 degrees ) tilt of actin subunits at high pH where filaments are readily disrupted. A second ADF molecule binds to a site on the opposite side of F-actin from that of the previously described ADF binding site, and this second site is only largely occupied at high pH. All of these states display a high degree of cooperativity that appears to be an integral part 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.