Arf1/COPI machinery acts directly on lipid droplets and enables their 
connection to the ER for protein targeting

Wilfling, Florian; Thiam, Abdou Rachid; Olarte, Maria-Jesus; Wang, Jing; Beck, Rainer; Gould, Travis J.; Allgeyer, Edward S.; Pincet, Frederic; Bewersdorf, Jörg; Farese, Robert V.; Walther, Tobias C.

doi:10.7554/eLife.01607

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Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting

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Citation

Wilfling, F., Thiam, A. R., Olarte, M.-J., Wang, J., Beck, R., Gould, T. J., et al. (2014). Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting. eLife, 3: e01607. doi:10.7554/eLife.01607.

Cite as: https://hdl.handle.net/21.11116/0000-0007-60DB-6

Abstract

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.