ArticleThe Journal of biological chemistry2025
Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks.
Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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
3 citing papers in PubMed.
- Review
- Inorganic phosphate rapidly switches the stability of Arp2/3-induced actin branches.The Journal of cell biology · 2026Article
- Coro1A and TRIM67 collaborate in netrin-dependent neuronal morphogenesis.The Journal of cell biology · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
The rapid turnover of branched actin networks underlies key in vivo processes such as lamellipodial extension, endocytosis, phagocytosis, and intracellular transport. However, our understanding of the mechanisms used to dissociate, or "prune," branched filaments has remained limited. Glia maturation factor (GMF) is a cofilin family protein that binds to the Arp2/3 complex and catalyzes branch dissociation. Here, we show that another ligand of Arp2/3 complex, Saccharomyces cerevisiae coronin (Crn1), enhances Gmf1-mediated debranching by 8- to 10-fold, and that these effects depend on Arp2/3-binding "C" and "A" motifs in Crn1. Further, we show that Crn1 directly binds with high affinity (K
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