ArticleNature structural & molecular biology2020
Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.
Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 62 citations in OpenAlex.
- Structural basis of Arpin homodimerization reveals cooperative inhibition of the Arp2/3 complex through dual-site engagement.Protein & cell · 2026Article
- Inorganic phosphate rapidly switches the stability of Arp2/3-induced actin branches.The Journal of cell biology · 2026Article
- Direct Actin Monomer Delivery is a WASP-specific Requirement for Arp2/3 Complex Activation.Journal of molecular biology · 2026Article
- Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025Article
- Activation of Arp2/3 complex by a SPIN90 dimer in linear actin-filament nucleation.Nature structural & molecular biology · 2025Article
- Akt-phosphorylated UFL1 UFMylates ArpC4 to promote metastasis.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
- From Molecules to Amoeboid Movement: A New Way for Understanding the Morphology Through Actin-Binding Proteins.Biomolecules · 2024Article
- We are junior scientists from emerging economies - the world needs more researchers like us solving global problems.Nature · 2024Article
- Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament.Nature structural & molecular biology · 2024Article
- Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex.Nature communications · 2024Article
- The stabilization of Arp2/3 complex generated actin filaments.Biochemical Society transactions · 2024Review
- Regeneration of actin filament branches from the same Arp2/3 complex.Science advances · 2024Article
- Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments.Nature structural & molecular biology · 2023Article
- Membrane-dependent actin polymerization mediated by the Legionella pneumophila effector protein MavH.PLoS pathogens · 2023Article
- Branching out in different directions: Emerging cellular functions for the Arp2/3 complex and WASP-family actin nucleation factors.European journal of cell biology · 2023Article
- Regulation of branched versus linear Arp2/3-generated actin filaments.The EMBO journal · 2023Article
- Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM.Biochemical Society transactions · 2023Review
- Membrane-dependent actin polymerization mediated by thebioRxiv : the preprint server for biology · 2023Article
- ArpC5 isoforms regulate Arp2/3 complex-dependent protrusion through differential Ena/VASP positioning.Science advances · 2023Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Arp2/3 complex, a crucial actin filament nucleator, undergoes structural rearrangements during activation by nucleation-promoting factors (NPFs). However, the conformational pathway leading to the nucleation-competent state is unclear due to lack of high-resolution structures of the activated state. Here we report a ~3.9 Å resolution cryo-EM structure of activated Schizosaccharomyces pombe Arp2/3 complex bound to the S. pombe NPF Dip1 and attached to the end of the nucleated actin filament. The structure reveals global and local conformational changes that allow the two actin-related proteins in Arp2/3 complex to mimic a filamentous actin dimer and template nucleation. Activation occurs through a clamp-twisting mechanism, in which Dip1 forces two core subunits in Arp2/3 complex to pivot around one another, shifting half of the complex into a new activated position. By showing how Dip1 stimulates activation, the structure reveals how NPFs can activate Arp2/3 complex in diverse cellular processes.
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