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. 2014:7:7-16.
doi: 10.4137/LPI.S11128.

Lipid Droplets as Signaling Platforms Linking Metabolic and Cellular Functions

Affiliations

Lipid Droplets as Signaling Platforms Linking Metabolic and Cellular Functions

Estela L Arrese et al. Lipid Insights. 2014.

Abstract

The main cells of the adipose tissue of animals, adipocytes, are characterized by the presence of large cytosolic lipid droplets (LDs), which store triglyceride (TG) and cholesterol. However, most cells have LDs and the ability to store lipids. LDs have a well-known central role in storage and provision of fatty acids and cholesterol. However, the complexity of the regulation of lipid metabolism on the surface of the LDs is still a matter of intense study. Beyond this role, a number of recent studies have suggested that LDs have major functions in other cellular processes, such as protein storage and degradation, and infection and immunity. Thus, our perception of LDs, from simple globules of fat to highly dynamic organelles of unexpected complexity, has been radically transformed. Here we compiled some recent evidence supporting the emerging view that LDs act as platforms connecting a number of relevant metabolic and cellular functions.

Keywords: Lipid droplet; fat body; lipid metabolism; lipoprotein; perilipin; triglycerides.

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Figures

Figure 1
Figure 1
Interaction among LDs, mitochondria, and ER. The transmission electron micrographs of M. sexta fat body show the physical contacts (indicated with arrows) observed between LD and mitochondria (A), or between LD and ER (B). This figure was adapted from a previous report and is reproduced with permission.
Figure 2
Figure 2
Changes in the protein composition of LDs from the same tissue. Protein profiles of purified LDs from the fat bodies of Manduca sexta larva and adult insects obtained by SDS-PAGE are shown in lanes 1 and 2, respectively. Additional information on the protein compositions of the LDs was previously reported. For comparison, the protein profile of Manduca sexta low density lipoprotein purified by ultracentrifugation in a density gradient is shown in the lane labeled LDLp. ApoLp-I, -II and -III refer to the protein components of the insect low density lipoprotein. Parts of the figure are reproduced from previous reports, with permission.

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