ArticleNature structural & molecular biology2025
Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- CARMIL membrane-binding domain regulates capping protein and actin assembly.The Journal of biological chemistry · 2026Article
- Direct Actin Monomer Delivery is a WASP-specific Requirement for Arp2/3 Complex Activation.Journal of molecular biology · 2026Article
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- Activation of Arp2/3 complex by a SPIN90 dimer in linear actin-filament nucleation.Nature structural & molecular biology · 2025Article
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Authors and funding
6 authors.
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Abstract
Branched actin networks nucleated by the Arp2/3 complex have critical roles in various cellular processes, from cell migration to intracellular transport. However, when activated by WISH/DIP/SPIN90-family proteins, Arp2/3 nucleates linear actin filaments. Here we found that human SPIN90 is a dimer that can nucleate bidirectional actin filaments. To understand the basis for this, we determined a 3-Å-resolution structure of human SPIN90-Arp2/3 complex nucleating actin filaments. Our structure shows that SPIN90 dimerizes through a three-helix bundle and interacts with two Arp2/3 complexes. Each SPIN90 molecule binds both Arp2/3 complexes to promote their activation. Our analysis demonstrates that single-filament nucleation by Arp2/3 is mechanistically more like branch formation than previously appreciated. The dimerization domain in SPIN90 orthologs is conserved in metazoans, suggesting that this mode of bidirectional nucleation is a common strategy to generate antiparallel actin filaments.
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