THESIS
2016
ix, 68 pages : illustrations (some color) ; 30 cm
Abstract
Lipid droplets (LDs) are organelles conserved for synthesizing, storing and supplying
lipid in eukaryotes. They consist of a neutral lipid core that is surrounded by a phospholipid
monolayer. Accumulating evidence suggests that the endoplasmic reticulum (ER) is in tight
association with LDs both physically and functionally during the biogenesis and expansion of
LDs. Seipin, encoded by the BSCL2 gene in human, is predicted to be an integral membrane
protein in the ER. Studies in yeast, Drosophila, mice and various cell lines suggest critical
roles for Seipin in regulating adipogenesis and LD morphology. However, the exact function
of Seipin remains poorly defined. Here we report that a functional GFP fusion protein of the
C. elegans Seipin ortholog (ceSeipin) is targeted to hithe...[
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Lipid droplets (LDs) are organelles conserved for synthesizing, storing and supplying
lipid in eukaryotes. They consist of a neutral lipid core that is surrounded by a phospholipid
monolayer. Accumulating evidence suggests that the endoplasmic reticulum (ER) is in tight
association with LDs both physically and functionally during the biogenesis and expansion of
LDs. Seipin, encoded by the BSCL2 gene in human, is predicted to be an integral membrane
protein in the ER. Studies in yeast, Drosophila, mice and various cell lines suggest critical
roles for Seipin in regulating adipogenesis and LD morphology. However, the exact function
of Seipin remains poorly defined. Here we report that a functional GFP fusion protein of the
C. elegans Seipin ortholog (ceSeipin) is targeted to hitherto uncharacterized cage structures
around a subset of LDs. Proper targeting of ceSeipin promotes the expansion of associated
LDs. Using genetics, biochemical assays and light microscopy, we have probed the molecular
basis of ceSeipin localization. In addition, we are using the CRISPR/Cas9 technique to
engineer precise mutations that are predicted to disrupt ceSeipin targeting. Further proteomic
studies will be performed to identify interacting partners of ceSeipin.
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