ArticleThe Journal of cell biology1997
Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
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Who cites it
93 citing papers in PubMed, 225 citations in OpenAlex.
- Control of microglial dynamics by the Arp2/3 complex and the autism- and schizophrenia-associated protein CYFIP1.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Actin-membrane interface stress regulates Arp2/3-branched actin density during lamellipodial protrusion.bioRxiv : the preprint server for biology · 2026Article
- 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
- Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks.The Journal of biological chemistry · 2025Article
- Myosin-based nucleation of actin filaments contributes to stereocilia development critical for hearing.Nature communications · 2025Article
- Machine learning-guided reconstruction of cytoskeleton network from live-cell AFM images.iScience · 2024Article
- Myosin-independent stiffness sensing by fibroblasts is regulated by the viscoelasticity of flowing actin.Communications materials · 2024Article
- GxcM-Fbp17/RacC-WASP signaling regulates polarized cortex assembly in migrating cells via Arp2/3.The Journal of cell biology · 2023Article
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- Calcium bursts allow rapid reorganization of EFhD2/Swip-1 cross-linked actin networks in epithelial wound closure.Nature communications · 2022Article
- Ventral stress fibers induce plasma membrane deformation in human fibroblasts.Molecular biology of the cell · 2021Article
- The cell pushes back: The Arp2/3 complex is a key orchestrator of cellular responses to environmental forces.Current opinion in cell biology · 2021Review
- The Arp2/3 Inhibitory Protein Arpin Is Required for Intestinal Epithelial Barrier Integrity.Frontiers in cell and developmental biology · 2021Article
- The Arp2/3 complex is crucial for colonisation of the mouse skin by melanoblasts.Development (Cambridge, England) · 2020Article
- Three-dimensional organization of the cytoskeleton: A cryo-electron tomography perspective.Protein science : a publication of the Protein Society · 2020Review
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- Profilin-Mediated Actin Allocation Regulates the Growth of Epithelial Microvilli.Current biology : CB · 2019Article
- TheBiology open · 2019Article
- A Cdc42 GEF, Gef1, through endocytosis organizes F-BAR Cdc15 along the actomyosin ring and promotes concentric furrowing.Journal of cell science · 2019Article
33 more citing papers are in PubMed but not listed here.
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3 authors at 1 institution in 1 country.
Funding
Abstract
The Arp2/3 complex, first isolated from Acanthamoeba castellani by affinity chromatography on profilin, consists of seven polypeptides; two actin-related proteins, Arp2 and Arp3; and five apparently novel proteins, p40, p35, p19, p18, and p14 (Machesky et al., 1994). The complex is homogeneous by hydrodynamic criteria with a Stokes' radius of 5.3 nm by gel filtration, sedimentation coefficient of 8.7 S, and molecular mass of 197 kD by analytical ultracentrifugation. The stoichiometry of the subunits is 1:1:1:1:1:1:1, indicating the purified complex contains one copy each of seven polypeptides. In electron micrographs, the complex has a bilobed or horseshoe shape with outer dimensions of approximately 13 x 10 nm, and mathematical models of such a shape and size are consistent with the measured hydrodynamic properties. Chemical cross-linking with a battery of cross-linkers of different spacer arm lengths and chemical reactivities identify the following nearest neighbors within the complex: Arp2 and p40; Arp2 and p35; Arp3 and p35; Arp3 and either p18 or p19; and p19 and p14. By fluorescent antibody staining with anti-p40 and -p35, the complex is concentrated in the cortex of the ameba, especially in linear structures, possibly actin filament bundles, that lie perpendicular to the leading edge. Purified Arp2/3 complex binds actin filaments with a Kd of 2.3 microM and a stoichiometry of approximately one complex molecule per actin monomer. In electron micrographs of negatively stained samples, Arp2/3 complex decorates the sides of actin filaments. EDC/NHS cross-links actin to Arp3, p35, and a low molecular weight subunit, p19, p18, or p14. We propose structural and topological models for the Arp2/3 complex and suggest that affinity for actin filaments accounts for the localization of complex subunits to actin-rich regions of Acanthamoeba.
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