ArticleProceedings of the National Academy of Sciences of the United States of America2010
An actin-filament-binding interface on the Arp2/3 complex is critical for nucleation and branch stability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 89 citations in OpenAlex.
- Ketogenic Diet-Associated Remodeling of the Cortical Proteome in Rats With Genetic Absence Epilepsy.Brain and behavior · 2026Article
- Direct Actin Monomer Delivery is a WASP-specific Requirement for Arp2/3 Complex Activation.Journal of molecular biology · 2026Article
- ARP2/3 protein complex regulates myoblast proliferation, morphology, migration, and fusion during embryonic chick skeletal myogenesis.In vitro cellular & developmental biology. Animal · 2026Article
- Akt-phosphorylated UFL1 UFMylates ArpC4 to promote metastasis.Nature structural & molecular biology · 2025Article
- The DNA Repair Component EEPD1 Regulates Actin Polymerization.Biology of the cell · 2025Article
- Protrusion-Derived Extracellular Vesicles (PD-EVs) and Their Diverse Origins: Key Players in Cellular Communication, Cancer Progression, and T Cell Modulation.Biology of the cell · 2025Review
- Simulated Microgravity-Induced Alterations in PDAC Cells: A Potential Role for Trichostatin A in Restoring Cellular Phenotype.International journal of molecular sciences · 2025Article
- Targeted Regulation of HSP70 by the ARP2/3 Complex in Mammary Epithelial Cells and Its Impact on Host Cell Apoptosis.Biomolecules · 2025Article
- DEHP (di(2-ethylhexyl)phthalate) stimulates skin pigmentation by perturbing cytoskeletal homeostasis.Toxicological research · 2024Article
- Liquid-like condensates mediate competition between actin branching and bundling.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Membrane tension induces F-actin reorganization and flow in a biomimetic model cortex.Communications biology · 2023Article
- Continuous dynamic identification of key genes and molecular signaling pathways of periosteum in guided bone self-generation in swine model.Journal of orthopaedic surgery and research · 2023Article
- Steps of actin filament branch formation by Arp2/3 complex investigated with coarse-grained molecular dynamics.Frontiers in cell and developmental biology · 2023Article
- Mechanism of actin filament branch formation by Arp2/3 complex revealed by a high-resolution cryo-EM structureof the branch junction.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Effect of GNE Mutations on Cytoskeletal Network Proteins: Potential Gateway to Understand Pathomechanism of GNEM.Neuromolecular medicine · 2022Article
- Article
- Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A recurrent,HGG advances · 2022Article
- Article
- Actin-related protein 2/3 complex plays a critical role in the aquaporin-2 exocytotic pathway.American journal of physiology. Renal physiology · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The Arp2/3 complex polymerizes new actin filaments from the sides of existing filaments, forming Y-branched networks that are critical for actin-mediated force generation. Binding of the Arp2/3 complex to the sides of actin filaments is therefore central to its actin-nucleating and branching activities. Although a model of the Arp2/3 complex in filament branches has been proposed based on electron microscopy, this model has not been validated using independent approaches, and the functional importance of predicted actin-binding residues has not been extensively tested. Using a combination of molecular dynamics and protein-protein docking simulations, we derived an independent structural model of the interaction between two subunits of the Arp2/3 complex that are key to actin binding, ARPC2 and ARPC4, and the side of an actin filament. This model agreed remarkably well with the previous results from electron microscopy. Complementary mutagenesis experiments revealed numerous residues in ARPC2 and ARPC4 that were required for the biochemical activity of the entire complex. Functionally critical residues clustered together and defined a surface that was predicted by protein-protein docking to be buried in the interaction with actin. Moreover, key residues at this interface were crucial for actin nucleation and Y-branching, high-affinity F-actin binding, and Y-branch stability, demonstrating that the affinity of Arp2/3 complex for F actin independently modulates branch formation and stability. Our results highlight the utility of combining computational and experimental approaches to study protein-protein interactions and provide a basis for further elucidating the role of F-actin binding in Arp2/3 complex activation and function.
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