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  COPI buds 60-nm lipid droplets from reconstituted water-phospholipid-triacylglyceride interfaces, suggesting a tension clamp function

Thiam, A. R., Antonny, B., Wang, J., Delacotte, J., Wilfling, F., Walther, T. C., et al. (2013). COPI buds 60-nm lipid droplets from reconstituted water-phospholipid-triacylglyceride interfaces, suggesting a tension clamp function. Proceedings of the National Academy of Sciences of the United States of America, 110(33), 13244-13249. doi:10.1073/pnas.1307685110.

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 Creators:
Thiam, Abdou Rachid1, Author
Antonny, Bruno1, Author
Wang, Jing1, Author
Delacotte, Jérôme1, Author
Wilfling, Florian2, Author                 
Walther, Tobias C.1, Author
Beck, Rainer1, Author
Rothman, James E.1, Author
Pincet, Frédéric1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Department of Cell Biology, Yale University School of Medicine, New Haven, Conneticut, USA, ou_persistent22              

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Free keywords: ADP-Ribosylation Factor 1, Animals, buffer-in-oil drops, Coat Protein Complex I, Escherichia coli, Humans, Hydrophobic and Hydrophilic Interactions, Lipid Bilayers, lipid droplet targetting, membrane tension, Microscopy, Electron, Phosphatidylcholines, Phosphatidylethanolamines, Phospholipids, Protein Transport, regulator, Sf9 Cells, Spectrometry, Fluorescence, Spodoptera, Surface Tension, Transport Vesicles, Triglycerides, Water
 Abstract: 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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Language(s): eng - English
 Dates: 2013-04-232013-07-032013-07-302013-08-13
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1307685110
BibTex Citekey: thiam_copi_2013
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 110 (33) Sequence Number: - Start / End Page: 13244 - 13249 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230