ArticleNature cell biology2025
P4-ATPases control phosphoinositide membrane asymmetry and neomycin resistance.
Article in Nature cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Lipid traffic: an enigmatic alliance between ORPs and a TMEM16-like protein at membrane contact sites.Biochemical Society transactions · 2026Review
- The lipid flippase MoNeo1 mediates vesicle trafficking and pathogenicity in Magnaporthe oryzae.Stress biology · 2026Article
- Article
- Distinct impact of PI(4)P flux on PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Ist2 promotes lipid transfer by Osh6 via its membrane tethering and lipid scramblase activities.Science advances · 2025Article
- A unique gating mechanism revealed by the cryo-EM structure of monomeric ATP9A flippase.The Journal of biological chemistry · 2025Article
- Phosphoinositide flipping governs neomycin sensitivity.Nature cell biology · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The aminoglycoside antibiotic neomycin has robust antibacterial properties, yet its clinical utility is curtailed by its nephrotoxicity and ototoxicity. The mechanism by which the polycationic neomycin enters specific eukaryotic cell types remains poorly understood. In budding yeast, NEO1 is required for neomycin resistance and encodes a phospholipid flippase that establishes membrane asymmetry. Here we show that mutations altering Neo1 substrate recognition cause neomycin hypersensitivity by exposing phosphatidylinositol-4-phosphate (PI4P) in the plasma membrane extracellular leaflet. Cryogenic electron microscopy reveals PI4P binding to Neo1 within the substrate translocation pathway. PI4P enters the lumen of the endoplasmic reticulum and is flipped by Neo1 at the Golgi to prevent PI4P secretion to the cell surface. Deficiency of the orthologous ATP9A in human cells also causes exposure of PI4P and neomycin sensitivity. These findings unveil conserved mechanisms of aminoglycoside sensitivity and phosphoinositide homoeostasis, with important implications for signalling by extracellular phosphoinositides.
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