ArticleScience advances2025
Steric repulsion counteracts ER-to-lipid droplet protein movement.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The trial behind it
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Who cites it
4 citing papers in PubMed.
- Perilipin-2-Anchored Lipid Droplet-Targeting Phototheranostics.Angewandte Chemie (International ed. in English) · 2026Article
- ATG2A-mediated DAG transfer recruits DGAT2 for lipid droplet growth.Nature structural & molecular biology · 2025Article
- "Seipin mediates Perilipin-1 recruitment to lipid droplets to preserve human adipocyte identity".bioRxiv : the preprint server for biology · 2025Article
- Navigating lipid droplet proteins - part II: molecular mechanisms underlying ER-to-lipid droplet protein partitioning.Biochemical Society transactions · 2025Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipid droplets (LDs) are organelles with a neutral lipid core surrounded by a phospholipid monolayer, which is continuous with the cytoplasmic leaflet of the endoplasmic reticulum (ER). LD function depends on a highly dynamic LD surface proteome. Key proteins continuously exchange between the ER and LDs; however, the mechanisms governing the interorganelle movement and accumulation on the LD surface remain poorly understood. Here, we developed an ex cellulo tool introducing a classification of ER-derived proteins based on their different affinity for LDs. We find that proteins with higher LD affinity can effectively displace those with lower affinity from the LD surface, identifying steric hindrance as a key mechanism in regulating ER-to-LD protein transfer. Consistent with this model, we show that, during adipocyte differentiation Plin1-an adipocyte-specific high-affinity LD protein-reduces the recruitment of ER proteins with lower affinity by displacing them from the LD surface. These findings highlight lateral protein-protein exclusion as a fundamental mechanism in shaping the LD proteome.
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Registered trials
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