ArticleNature communications2020
Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed.
- Inorganic phosphate rapidly switches the stability of Arp2/3-induced actin branches.The Journal of cell biology · 2026Article
- The membrane-to-cortex distance regulates mDia1 activity to control cortical mechanics.Nature communications · 2026Article
- Recent insights into the plant ARP2/3 complex.Protoplasma · 2026Review
- Cryo-electron tomography reveals OmpB is required for themicroPublication biology · 2026Article
- 4-phenylbutyric acid alleviated sepsis-induced myocardial dysfunction by inhibition of MAM formation to improve mitochondrial dynamic balance in myocardial cells.Burns & trauma · 2026Article
- Mechanism of Arp2/3 complex branch disassembly by human Coro7.Nature communications · 2025Article
- 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
- Article
- An atypical Arp2/3 complex is required for Plasmodium DNA segregation and malaria transmission.Nature microbiology · 2025Article
- Cryo-ET of actin cytoskeleton and membrane structure in lamellipodia formation using optogenetics.iScience · 2025Article
- Functional divergence of plant SCAR/WAVE proteins is determined by intrinsically disordered regions.Science advances · 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
- NPF binding to Arp2 is allosterically linked to the release of ArpC5's N-terminal tail and conformational changes in Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Comparing simulations of actin filament compression reveals tradeoff between computational cost and capturing supertwist.microPublication biology · 2025Article
- MST1 interactomes profiling across cell death in esophageal squamous cell carcinoma.Medical review (2021) · 2024Article
- MiLoPYP: self-supervised molecular pattern mining and particle localization in situ.Nature methods · 2024Article
- 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
- Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex.Nature communications · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The actin-related protein (Arp)2/3 complex nucleates branched actin filament networks pivotal for cell migration, endocytosis and pathogen infection. Its activation is tightly regulated and involves complex structural rearrangements and actin filament binding, which are yet to be understood. Here, we report a 9.0 Å resolution structure of the actin filament Arp2/3 complex branch junction in cells using cryo-electron tomography and subtomogram averaging. This allows us to generate an accurate model of the active Arp2/3 complex in the branch junction and its interaction with actin filaments. Notably, our model reveals a previously undescribed set of interactions of the Arp2/3 complex with the mother filament, significantly different to the previous branch junction model. Our structure also indicates a central role for the ArpC3 subunit in stabilizing the active conformation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.