Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting
Copyright policy )Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting
Lipid droplets (LDs) are ubiquitous organelles that store neutral lipids, such as triacylglycerol (TG), as reservoirs of metabolic energy and membrane precursors. The Arf1/COPI protein machinery, known for its role in vesicle trafficking, regulates LD morphology, targeting of specific proteins to LDs and lipolysis through unclear mechanisms. Recent evidence shows that Arf1/COPI can bud nano-LDs (∼60 nm diameter) from phospholipid-covered oil/water interfaces in vitro. We show that Arf1/COPI proteins localize to cellular LDs, are sufficient to bud nano-LDs from cellular LDs, and are required for targeting specific TG-synthesis enzymes to LD surfaces. Cells lacking Arf1/COPI function have increased amounts of phospholipids on LDs, resulting in decreased LD surface tension and impairment to form bridges to the ER. Our findings uncover a function for Arf1/COPI proteins at LDs and suggest a model in which Arf1/COPI machinery acts to control ER-LD connections for localization of key enzymes of TG storage and catabolism.
- Sorbonne University France
- CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE France
- University of Paris France
- Heidelberg University Germany
- Sorbonne Paris Cité France
Time Factors, QH301-705.5, Science, Lipolysis, lipid droplet, ER-lipid droplet connection, triglyceride synthesis, Endoplasmic Reticulum, Transfection, Biochemistry, Cell Line, Coat Protein Complex I, ER-lipid droplet connections, Mice, protein targeting, Animals, Drosophila Proteins, Humans, Surface Tension, Biology (General), Particle Size, Phospholipids, Triglycerides, Q, R, Biological Transport, Lipase, Lipid Droplets, [SDV] Life Sciences [q-bio], Drosophila melanogaster, lipolysis, Medicine, Nanoparticles, ADP-Ribosylation Factor 1, RNA Interference, COP-Coated Vesicles
Time Factors, QH301-705.5, Science, Lipolysis, lipid droplet, ER-lipid droplet connection, triglyceride synthesis, Endoplasmic Reticulum, Transfection, Biochemistry, Cell Line, Coat Protein Complex I, ER-lipid droplet connections, Mice, protein targeting, Animals, Drosophila Proteins, Humans, Surface Tension, Biology (General), Particle Size, Phospholipids, Triglycerides, Q, R, Biological Transport, Lipase, Lipid Droplets, [SDV] Life Sciences [q-bio], Drosophila melanogaster, lipolysis, Medicine, Nanoparticles, ADP-Ribosylation Factor 1, RNA Interference, COP-Coated Vesicles
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