ArticleThe EMBO journal2018
Structure of the nucleation-promoting factor SPIN90 bound to the actin filament nucleator Arp2/3 complex.
Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- 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
- CK-666 and CK-869 differentially inhibit Arp2/3 iso-complexes.EMBO reports · 2024Article
- Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament.Nature structural & molecular biology · 2024Article
- The stabilization of Arp2/3 complex generated actin filaments.Biochemical Society transactions · 2024Review
- 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
- Regulation of branched versus linear Arp2/3-generated actin filaments.The EMBO journal · 2023Article
- Small GTPase Cdc42, WASP, and scaffold proteins for higher-order assembly of the F-BAR domain protein.Science advances · 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
- Analysis of functional surfaces on the actin nucleation promoting factor Dip1 required for Arp2/3 complex activation and endocytic actin network assembly.The Journal of biological chemistry · 2022Article
- 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
- Mechanistic insights into actin force generation during vesicle formation from cryo-electron tomography.Developmental cell · 2022Article
- 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
- Article
- Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms.Biology open · 2020Article
- SPIN90 associates with mDia1 and the Arp2/3 complex to regulate cortical actin organization.Nature cell biology · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Unlike the WASP family of Arp2/3 complex activators, WISH/DIP/SPIN90 (WDS) family proteins activate actin filament nucleation by the Arp2/3 complex without the need for a preformed actin filament. This allows WDS proteins to initiate branched actin network assembly by providing seed filaments that activate WASP-bound Arp2/3 complex. Despite their important role in actin network initiation, it is unclear how WDS proteins drive the activating steps that require both WASP and pre-existing actin filaments during WASP-mediated nucleation. Here, we show that SPIN90 folds into an armadillo repeat domain that binds a surface of Arp2/3 complex distinct from the two WASP sites, straddling a hinge point that may stimulate movement of the Arp2 subunit into the activated short-pitch conformation. SPIN90 binds a surface on Arp2/3 complex that overlaps with actin filament binding, explaining how it could stimulate the same structural rearrangements in the complex as pre-existing actin filaments. By revealing how WDS proteins activate the Arp2/3 complex, these data provide a molecular foundation to understand initiation of dendritic actin networks and regulation of Arp2/3 complex by its activators.
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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 OpenQuestion graph.