ArticleProceedings of the National Academy of Sciences of the United States of America1998
The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 611 papers, 1 of them a synthesis that pooled it.
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
611 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,428 citations in OpenAlex.
- A meta-analysis indicates that the regulation of cell motility is a non-intrinsic function of chemoattractant receptors that is governed independently of directional sensing.Frontiers in immunology · 2022Pooled it
- A specialized CD107aiScience · 2026Article
- Actin conformation dynamics precede force generation in cytotoxic T lymphocytes.Communications biology · 2026Article
- Distinct Arp2/3 isocomplexes drive axonal actin ring assembly and integrity.Science advances · 2026Article
- Article
- The membrane-to-cortex distance regulates mDia1 activity to control cortical mechanics.Nature communications · 2026Article
- Alterations of actin in aging.Journal of cell science · 2026Review
- Arf1 is involved in Neisseria meningitidis-induced cortical branched F-actin network reorganization.EMBO reports · 2026Article
- Proteomic Analysis of Paraffin-Embedded Intestines fromProteomes · 2026Article
- Regulation of CFTR stability at the plasma membrane-Mechanisms and therapeutic opportunities in cystic fibrosis.FEBS letters · 2026Review
- Agent-Based Computational Modeling of the Stochastic Dynamic Behavior of Actin Filaments Recapitulates the Homeostatic Cortical Array in Plant Epidermal Cells.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Recent insights into the plant ARP2/3 complex.Protoplasma · 2026Review
- Arp2/3 involvement in intercellular bridge membrane fluctuations and constriction during neural stem cell divisions.iScience · 2026Article
- Characterisation of a Leaky Splice-Site Mutation Associated with Phenotypic Diversity in Two Unrelated Patients with ARPC1B Deficiency.Journal of clinical immunology · 2026Article
- Synaptic spine head morphodynamics from graph grammar rules for actin dynamics.bioRxiv : the preprint server for biology · 2026Article
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- Coordinated Arp2/3-mediated actin branching and myosin-dependent force generation in membrane-cytoskeleton remodeling.Frontiers in physiology · 2026Review
- Rotational migration in human pancreatic ductal organoids depends on actin and myosin activity.Communications biology · 2025Article
- Mechanical Signaling: Molecular Mechanisms, Biological Functions, Diseases, and Therapeutic Targets.MedComm · 2025Review
- Ubiquitylation-dependent Rap2 activation regulates lamellipodia dynamics during cell migration.Journal of cell science · 2025Article
551 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Arp2/3 complex is a stable assembly of seven protein subunits including two actin-related proteins (Arp2 and Arp3) and five novel proteins. Previous work showed that this complex binds to the sides of actin filaments and is concentrated at the leading edges of motile cells. Here, we show that Arp2/3 complex purified from Acanthamoeba caps the pointed ends of actin filaments with high affinity. Arp2/3 complex inhibits both monomer addition and dissociation at the pointed ends of actin filaments with apparent nanomolar affinity and increases the critical concentration for polymerization at the pointed end from 0.6 to 1.0 microM. The high affinity of Arp2/3 complex for pointed ends and its abundance in amoebae suggest that in vivo all actin filament pointed ends are capped by Arp2/3 complex. Arp2/3 complex also nucleates formation of actin filaments that elongate only from their barbed ends. From kinetic analysis, the nucleation mechanism appears to involve stabilization of polymerization intermediates (probably actin dimers). In electron micrographs of quick-frozen, deep-etched samples, we see Arp2/3 bound to sides and pointed ends of actin filaments and examples of Arp2/3 complex attaching pointed ends of filaments to sides of other filaments. In these cases, the angle of attachment is a remarkably constant 70 +/- 7 degrees. From these in vitro biochemical properties, we propose a model for how Arp2/3 complex controls the assembly of a branching network of actin filaments at the leading edge of motile cells.
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.