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Abstract
Cytoplasmic lipid droplets are highly dynamic storage organelles that are critical for cellular lipid homeostasis. While the molecular details of lipid droplet dynamics are a very active area of investigation, this work has been primarily performed in cultured cells. Taking advantage of the powerful transgenic and in vivo imaging opportunities available in zebrafish, we built a suite of tools to study lipid droplets in real time from the subcellular to the whole organism level. Fluorescently tagging the lipid droplet-associated proteins, perilipin 2 and perilipin 3, in the endogenous loci permits visualization of lipid droplets in the intestine, liver, and adipose tissue. Using these tools, we found that perilipin 3 is rapidly loaded on intestinal lipid droplets following a high-fat meal and later replaced by perilipin 2. These powerful new tools will facilitate studies on the role of lipid droplets in different tissues, under different genetic and physiological manipulations, and in a variety of human disease models.
Highlights
Lipid droplets are typically coated by one or more perilipins, an evolutionarily related protein family defined by two conserved protein motifs, the N-terminal ~100 amino acid hydrophobic PAT domain followed by a repeating 11-mer helical motif of varying length (Kimmel and Sztalryd, 2016)
PLIN4 is expressed in adipocytes, brain, heart and skeletal muscle, and PLIN5 is found in fatty acid oxidizing tissues such as heart, brown adipose tissue, and skeletal muscle, as well as in the liver (Dalen et al, 2007; Wolins et al, 2006; Yamaguchi et al, 2006)
We describe the ordered recruitment of plin3 and plin2 to lipid droplets in intestinal enterocytes following the consumption of a high fat meal, reveal a delay in hepatic expression of plin2 and plin3 during development and identify a population of plin2-positive lipid droplets adjacent to neuromasts in the posterior lateral line
Summary
Lipid droplets are typically coated by one or more perilipins, an evolutionarily related protein family defined by two conserved protein motifs, the N-terminal ~100 amino acid hydrophobic PAT domain followed by a repeating 11-mer helical motif of varying length (Kimmel and Sztalryd, 2016). Neither plin2 nor plin3 mRNA expression was noted in the liver or in other tissues of unfed or high-fat fed zebrafish larvae at 6 dpf Fish carrying the knock-in alleles can be in-crossed and resulting progeny express RFP-plin3 in the intestine prior to feeding and both transgenes are expressed subsequent to consuming a high-fat meal (Figure 1F).
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