ArticlePLoS computational biology2011
Phosphorylation of the Arp2 subunit relieves auto-inhibitory interactions for Arp2/3 complex activation.
Article in PLoS computational biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation.Biochemistry · 2022Review
- Wnt5A signaling supports antigen processing and CD8 T cell activation.Frontiers in immunology · 2022Article
- Wnt5A-Mediated Actin Organization Regulates Host Response to Bacterial Pathogens and Non-Pathogens.Frontiers in immunology · 2020Article
- Effects of Acetylation and Phosphorylation on Subunit Interactions in Three Large Eukaryotic Complexes.Molecular & cellular proteomics : MCP · 2018Article
- Phosphorylation of Arp2 is not essential for Arp2/3 complex activity in fission yeast.Life science alliance · 2018Article
- Article
- Identification of an ATP-controlled allosteric switch that controls actin filament nucleation by Arp2/3 complex.Nature communications · 2016Article
- Role and structural mechanism of WASP-triggered conformational changes in branched actin filament nucleation by Arp2/3 complex.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Non-degradative Ubiquitination of Protein Kinases.PLoS computational biology · 2016Article
- Article
- The Nck-interacting kinase NIK increases Arp2/3 complex activity by phosphorylating the Arp2 subunit.The Journal of cell biology · 2015Article
- Response of rat lung tissue to short-term hyperoxia: a proteomic approach.Molecular and cellular biochemistry · 2013Article
- Phosphorylation of actin-related protein 2 (Arp2) is required for normal development and cAMP chemotaxis in Dictyostelium.The Journal of biological chemistry · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Actin filament assembly by the actin-related protein (Arp) 2/3 complex is necessary to build many cellular structures, including lamellipodia at the leading edge of motile cells and phagocytic cups, and to move endosomes and intracellular pathogens. The crucial role of the Arp2/3 complex in cellular processes requires precise spatiotemporal regulation of its activity. While binding of nucleation-promoting factors (NPFs) has long been considered essential to Arp2/3 complex activity, we recently showed that phosphorylation of the Arp2 subunit is also necessary for Arp2/3 complex activation. Using molecular dynamics simulations and biochemical assays with recombinant Arp2/3 complex, we now show how phosphorylation of Arp2 induces conformational changes permitting activation. The simulations suggest that phosphorylation causes reorientation of Arp2 relative to Arp3 by destabilizing a network of salt-bridge interactions at the interface of the Arp2, Arp3, and ARPC4 subunits. Simulations also suggest a gain-of-function ARPC4 mutant that we show experimentally to have substantial activity in the absence of NPFs. We propose a model in which a network of auto-inhibitory salt-bridge interactions holds the Arp2 subunit in an inactive orientation. These auto-inhibitory interactions are destabilized upon phosphorylation of Arp2, allowing Arp2 to reorient to an activation-competent state.
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Registered trials
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