期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 33, 页码 13244-13249出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1307685110
关键词
regulator; membrane tension; lipid droplet targetting; buffer-in-oil drops
资金
- Marie Curie Budding and Fusion of Lipid Droplets International Outgoing Fellowship within the Seventh European Community Framework Program
- Yale University [268888]
- National Institutes of Health Grant [R01GM097194]
- Ecole Normale Superieure laboratories [268888]
- European Research Council [268888]
- European Research Council (ERC) [268888] Funding Source: European Research Council (ERC)
Intracellular trafficking between organelles is achieved by coat protein complexes, coat protomers, that bud vesicles from bilayer membranes. Lipid droplets are protected by a monolayer and thus seem unsuitable targets for coatomers. Unexpectedly, coat protein complex I (COPI) is required for lipid droplet targeting of some proteins, suggesting a possible direct interaction between COPI and lipid droplets. Here, we find that COPI coat components can bud 60-nm triacylglycerol nanodroplets from artificial lipid droplet (LD) interfaces. This budding decreases phospholipid packing of the monolayer decorating the mother LD. As a result, hydrophobic triacylglycerol molecules become more exposed to the aqueous environment, increasing LD surface tension. In vivo, this surface tension increase may prime lipid droplets for reactions with neighboring proteins or membranes. It provides a mechanism fundamentally different from transport vesicle formation by COPI, likely responsible for the diverse lipid droplet phenotypes associated with depletion of COPI subunits.
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