ArticleProceedings of the National Academy of Sciences of the United States of America2018
Identification of Wiskott-Aldrich syndrome protein (WASP) binding sites on the branched actin filament nucleator Arp2/3 complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 36 citations in OpenAlex.
- Exploring roles for essential proteins in yeast filamentous growth identifies the WASP homolog Las17 as a regulator of the Cdc42-dependent fMAPK pathway.bioRxiv : the preprint server for biology · 2026Article
- Subcellular Stress Markers in Epithelial Ovarian Cancer.International journal of molecular sciences · 2025Review
- Activation of Arp2/3 complex by a SPIN90 dimer in linear actin-filament nucleation.Nature structural & molecular biology · 2025Article
- Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025Review
- A first-in-class Wiskott-Aldrich syndrome protein activator with antitumor activity in hematologic cancers.Haematologica · 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
- Mechanism of synergistic activation of Arp2/3 complex by cortactin and WASP-family proteins.Nature communications · 2023Article
- Transition State of Arp2/3 Complex Activation by Actin-Bound Dimeric Nucleation-Promoting Factor.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Liquid-like condensates mediate competition between actin branching and bundling.bioRxiv : the preprint server for biology · 2023Article
- Steps of actin filament branch formation by Arp2/3 complex investigated with coarse-grained molecular dynamics.Frontiers in cell and developmental biology · 2023Article
- Mechanical Forces Govern Interactions of Host Cells with Intracellular Bacterial Pathogens.Microbiology and molecular biology reviews : MMBR · 2022Review
- Nucleation, stabilization, and disassembly of branched actin networks.Trends in cell biology · 2022Review
- Unconcerted conformational changes in Arp2/3 complex integrate multiple activating signals to assemble functional actin networks.Current biology : CB · 2022Article
- The Actin Regulators Involved in the Function and Related Diseases of Lymphocytes.Frontiers in immunology · 2022Review
- Targeting the actin nucleation promoting factor WASp provides a therapeutic approach for hematopoietic malignancies.Nature communications · 2021Article
- Review
- Profilin's Affinity for Formin Regulates the Availability of Filament Ends for Actin Monomer Binding.Journal of molecular biology · 2020Article
- Article
- Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.Nature structural & molecular biology · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Arp2/3 complex nucleates branched actin filaments important for cellular motility and endocytosis. WASP family proteins are Arp2/3 complex activators that play multiple roles in branching nucleation, but little is known about the structural bases of these WASP functions, owing to an incomplete understanding of how WASP binds Arp2/3 complex. Recent data show WASP binds two sites, and biochemical and structural studies led to models in which the WASP C segment engages the barbed ends of the Arp3 and Arp2 subunits while the WASP A segment binds the back side of the complex on Arp3. However, electron microscopy reconstructions showed density for WASP inconsistent with these models on the opposite (front) side of Arp2/3 complex. Here we use chemical cross-linking and mass spectrometry (XL-MS) along with computational docking and structure-based mutational analysis to map the two WASP binding sites on the complex. Our data corroborate the barbed end and back side binding models and show one WASP binding site on Arp3, on the back side of the complex, and a second site on the bottom of the complex, spanning Arp2 and ARPC1. The XL-MS-identified cross-links rule out the front side binding model and show that the A segment of WASP binds along the bottom side of the ARPC1 subunit, instead of at the Arp2/ARPC1 interface, as suggested by FRET experiments. The identified binding sites support the Arp3 tail release model to explain WASP-mediated activating conformational changes in Arp2/3 complex and provide insight into the roles of WASP in branching nucleation.
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