ArticleJournal of cell science2025
Functional requirements of the liver isoform of phosphofructokinase-1 in breast cancer cell migration.
Article in Journal of cell science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- High-Speed AFM Reveals Ligand-Dependent Supramolecular Switching of Human Phosphofructokinase-1.Research square · 2026Article
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Authors and funding
2 authors.
Funding
Abstract
Increased aerobic glycolysis and increased cell motility are hallmarks of metastatic cancer. Migrating cancer cells are highly polarized, suggesting that glycolytic enzymes could be spatially regulated. Here, we investigated the role of the liver isoform of the 'gatekeeper' glycolytic enzyme phosphofructokinase-1 (PFKL) in breast cancer cell migration. Depletion of PFKL significantly decreased migration velocity and directional sensing. We have observed the localization of PFKL to lamellipodia of migrating breast cancer cells, where it colocalized with hexokinase-2 and pyruvate kinase M2. We then investigated the functional requirements of PFKL for directional migration. First, we found that expression of catalytically inactive PFKL or indirect pharmacological inhibition of PFKL activity significantly decreased directional migration. Second, we discovered that disrupting PFKL filament formation by expression of a filament-incompetent mutant decreased PFKL recruitment to lamellipodia and directional sensing, without altering migration velocity. These findings indicate that both catalytic activity and subcellular localization are required for directional migration in breast cancer cells. These results suggest a novel function of PFKL filaments in cells and provide insight into the function of compartmentalized glycolysis in the cytoplasm.
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