ArticleDevelopmental cell2025
ER nests are specialized ER subdomains in Arabidopsis where peroxisomes and lipid droplets form.
Article in Developmental cell, 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.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Getting nuclear size just right - emerging mechanisms regulating nuclear scaling and morphology.Journal of cell science · 2026Review
- PEX11 mediates intralumenal vesicle formation in peroxisomes.Nature communications · 2026Article
- Lipid droplets at the interface of plant defense and pathogen exploitation.Frontiers in plant science · 2026Review
- Move over endosymbionts, peroxisomes pass electrons too.Biochemical Society transactions · 2025Review
- Identifying and characterizing a missing peroxin-PEX8-in Arabidopsis thaliana.The Plant cell · 2025Article
- Restoring metabolic flexibility: targeting organelle interaction networks in the pathogenesis and therapy of MASLD.Frontiers in cell and developmental biology · 2025Review
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Authors and funding
3 authors.
Funding
Abstract
Organelles are defining features of eukaryotic cells, yet much remains to be learned about organelle biogenesis. Lipid droplets and peroxisomes, which play opposing roles in storing and catabolizing fats, form from a mysterious domain in the endoplasmic reticulum (ER). We used live-cell fluorescence microscopy to visualize peroxisome and lipid droplet biogenesis in young Arabidopsis seedlings, where lipid catabolism is active, and peroxisomes can be unusually large. We found that the ER domains where these organelles are born, which we term ER nests, are complex, dynamic structures that exclude general ER proteins but accumulate other proteins, including lipid biosynthetic enzymes and the COPII component SAR1. Furthermore, ER nests appear to define peroxisome-lipid droplet contact sites. Our findings provide a framework for understanding how these domains form and sort their protein components, illuminate eukaryotic lipid biosynthesis, and elucidate how distinct organelles arise from the ER.
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