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First published online May 20, 2009


Journal of Cell Science 122, 1104e (2009)
© The Company of Biologists Limited
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In this issue

Special delivery – lipid-droplet proteins


Figure 1

Lipid droplets consist of a neutral lipid core bound by a phospholipid monolayer and several different types of lipid-droplet-associated proteins (LDAPs), including adipose triglyceride lipase (ATGL) and the PAT-domain-family proteins ADRP and TIP47. Although it is generally accepted that lipid droplets derive from the ER, how LDAPs become associated with lipid droplets was unclear. On page 1834, Juan Bonifacino and colleagues now define a pathway by which some LDAPs are targeted to nascent lipid droplets. In this study, they show that inhibiting ER-Golgi transport with brefeldin A prevents the association of ATGL with newly formed lipid droplets, and that this causes alterations in their lipid composition and morphology. Furthermore, individual components of the ER-Golgi transport machinery – including GBF1, ARF1 and coatomer protein I (COPI) – are required for optimal association of ATGL with lipid droplets. COPII, another protein complex that is involved in protein export from the ER, is also involved in delivering ATGL to lipid droplets, although to a lesser extent than COPI. Importantly, the finding that the targeting of ADRP, but not TIP47, occurs via the same brefeldin-A-sensitive pathway as that of ATGL suggests that there is more than one pathway involved in targeting LDAPs to nascent lipid droplets.


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Related articles in JCS:

Coatomer-dependent protein delivery to lipid droplets
Krishnakant G. Soni, Gonzalo A. Mardones, Rachid Sougrat, Elena Smirnova, Catherine L. Jackson, and Juan S. Bonifacino
JCS 2009 122: 1834-1841. [Abstract] [Full Text]  




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