ArticleThe Journal of cell biology2025
Any1 is a phospholipid scramblase involved in endosome biogenesis.
Article in The Journal of cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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
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Who cites it
6 citing papers in PubMed.
- Lipid flip-flop in biological membranes: through the lens of TMEM16F.Physiological reviews · 2026Review
- TMEM170 proteins are lipid scramblases associated with bridge-type lipid transporters BLTP1/Csf1.Nature structural & molecular biology · 2026Article
- Classification and biogenesis of vesicles, and their roles in the transport of viral components.Archives of microbiology · 2026Review
- The endo-lysosomal-lipid axis: bidirectional interactions between membrane trafficking dysfunction and lipid metabolic disorders.Frontiers in cell and developmental biology · 2026Review
- Martini 3 Limitations in Phospholipid Flip-Flop.Journal of chemical theory and computation · 2025Article
- The SLC-ome of membrane transport: From molecular discovery to physiology and clinical applications.Physiological reviews · 2025Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Endosomes are central organelles in the recycling and degradation of receptors and membrane proteins. Once endocytosed, such proteins are sorted at endosomes into intraluminal vesicles (ILVs). The resulting multivesicular bodies (MVBs) then fuse with the lysosomes, leading to the degradation of ILVs and recycling of the resulting monomers. However, the biogenesis of MVBs requires a constant lipid supply for efficient ILV formation. An ER-endosome membrane contact site has been suggested to play a critical role in MVB biogenesis. Here, we identify Any1 as a novel phospholipid scramblase, which functions with the lipid transfer protein Vps13 in MVB biogenesis. We uncover that Any1 cycles between the early endosomes and the Golgi and colocalizes with Vps13, possibly at a here-discovered potential contact site between lipid droplets (LDs) and endosomes. Strikingly, both Any1 and Vps13 are required for MVB formation, presumably to couple lipid flux with membrane homeostasis during ILV formation and endosome maturation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.