ArticleThe Journal of cell biology2026
Inorganic phosphate rapidly switches the stability of Arp2/3-induced actin branches.
Article in The Journal of cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Physical confinement modulates the rate-limiting transition in the release of phosphate from actin filaments.Science advances · 2026Article
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Authors and funding
10 authors.
Funding
Abstract
Actin filaments often appear as branches, nucleated by the Arp2/3 complex. Arp2 and Arp3 are ATPases, which adopt different nucleotide-dependent conformations. We investigated how the nucleotide state of mammalian Arp2/3 complexes affects branch stability, by applying mechanical load. Branch junctions are 30-fold more stable when Arp2/3 is in the ADP-inorganic phosphate (Pi) rather than the ADP state. Pi is in rapid equilibrium with the ADP-Arp2/3 complex at the branch junction (release rate 0.2 s-1). Upon branch dissociation, Arp2/3 complexes remaining attached to the mother filament in the ADP-Pi state are 100-fold more stable, release their phosphate slowly (0.05 s-1), and can regrow branches without reloading ATP. Glia maturation factor (GMF) accelerates the dissociation of surviving ADP-Arp2/3 complexes, but does not prevent branch regrowth at physiological ATP concentration. Cortactin stabilizes branches and enhances renucleation. Neither GMF nor cortactin affects branch stability and renucleation of ADP-Pi-Arp2/3. Overall, these results identify Pi in the Arp2/3 complex as a critical regulator of branched actin network stability.
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