ArticleNature communications2016
Identification of an ATP-controlled allosteric switch that controls actin filament nucleation by Arp2/3 complex.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Caspase-3/Drice as a critical regulator of actin dynamics through its dual control of small RhoGTPase family and Gelsolin in the Malpighian tubules of Drosophila.Cell death discovery · 2026Article
- Direct Actin Monomer Delivery is a WASP-specific Requirement for Arp2/3 Complex Activation.Journal of molecular biology · 2026Article
- Mechanism of Arp2/3 complex branch disassembly by human Coro7.Nature communications · 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
- The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025Review
- Evolutionary diversification reveals distinct somatic versus germline cytoskeletal functions of the Arp2 branched actin nucleator protein.Current biology : CB · 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
- Steps of actin filament branch formation by Arp2/3 complex investigated with coarse-grained molecular dynamics.Frontiers in cell and developmental biology · 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
- 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
- Unconcerted conformational changes in Arp2/3 complex integrate multiple activating signals to assemble functional actin networks.Current biology : CB · 2022Article
- Molecular mechanism of Arp2/3 complex inhibition by Arpin.Nature communications · 2022Article
- Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction.Nature communications · 2020Article
- Article
- Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.Nature structural & molecular biology · 2020Article
- Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms.Biology open · 2020Article
- Partial loss of actin nucleator actin-related protein 2/3 activity triggers blebbing in primary T lymphocytes.Immunology and cell biology · 2020Article
- Single-Turnover Activation of Arp2/3 Complex by Dip1 May Balance Nucleation of Linear versus Branched Actin Filaments.Current biology : CB · 2019Article
- Stoichiometry controls activity of phase-separated clusters of actin signaling proteins.Science (New York, N.Y.) · 2019Article
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5 authors at 1 institution in 1 country.
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Abstract
Nucleation of branched actin filaments by Arp2/3 complex is tightly regulated to control actin assembly in cells. Arp2/3 complex activation involves conformational changes brought about by ATP, Nucleation Promoting Factor (NPF) proteins, actin filaments and NPF-recruited actin monomers. To understand how these factors promote activation, we must first understand how the complex is held inactive in their absence. Here we demonstrate that the Arp3 C-terminal tail is a structural switch that prevents Arp2/3 complex from adopting an active conformation. The interaction between the tail and a hydrophobic groove in Arp3 blocks movement of Arp2 and Arp3 into an activated filament-like (short pitch) conformation. Our data indicate ATP binding destabilizes this interaction via an allosteric link between the Arp3 nucleotide cleft and the hydrophobic groove, thereby promoting the short-pitch conformation. Our results help explain how Arp2/3 complex is locked in an inactive state without activators and how autoinhibition is relieved.
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