ArticleNature communications2024
Phalloidin and DNase I-bound F-actin pointed end structures reveal principles of filament stabilization and disassembly.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Disruption of dopamine transmission by cholesterol depletion is associated with alterations in protein lipid raft partitioning and actin dynamics.Neuropharmacology · 2026Article
- Functional analysis of down-regulated CYP6AE gene clusters involved in the insecticidal mechanism of lycorine against Spodoptera litura.Pest management science · 2026Article
- Study of Cytotoxicity of Pyrrolo[3,4-International journal of molecular sciences · 2026Article
- Structural mechanisms of drebrin-mediated F-actin network modulation.Nature communications · 2026Article
- DNase I as a probe for unpolymerized actin: revisiting a classic tool for nuclear actin research.Pflugers Archiv : European journal of physiology · 2026Review
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- SH3BGRL proteins are thioredoxin fold-containing actin filament pointed end capping proteins (TPECs).Scientific reports · 2026Article
- The structure of an actin nucleus stabilized by villin.Science advances · 2025Article
- Reaching the full potential of cryo-EM reconstructions with molecular dynamics simulations at 310 K: Actin filaments as an example.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Degradation rather than disassembly of necrotic debris is essential to enhance recovery after acute liver injury.Cellular and molecular life sciences : CMLS · 2025Article
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Authors and funding
5 authors.
Funding
Abstract
Actin filament turnover involves subunits binding to and dissociating from the filament ends, with the pointed end being the primary site of filament disassembly. Several molecules modulate filament turnover, but the underlying mechanisms remain incompletely understood. Here, we present three cryo-EM structures of the F-actin pointed end in the presence and absence of phalloidin or DNase I. The two terminal subunits at the undecorated pointed end adopt a twisted conformation. Phalloidin can still bind and bridge these subunits, inducing a conformational shift to a flattened, F-actin-like state. This explains how phalloidin prevents depolymerization at the pointed end. Interestingly, two DNase I molecules simultaneously bind to the phalloidin-stabilized pointed end. In the absence of phalloidin, DNase I binding would disrupt the terminal actin subunit packing, resulting in filament disassembly. Our findings uncover molecular principles of pointed end regulation and provide structural insights into the kinetic asymmetry between the actin filament ends.
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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 Socratic graph.