THESIS
2015
x, 52 pages : illustrations (some color) ; 30 cm
Abstract
Lipid droplets (LDs) are conserved organelles for cellular fat storage. In C.elegans,
numerous LDs can be found in intestinal cells, where fat is primarily stored. Proteomic
studies have identified a large set of LD associated proteins. However, mechanisms
governing the targeting and turnover of these proteins are largely unknown. Our lab has
previously identified DGAT-2 as a LD associated protein in C.elegans. DGAT-2 is an acyl-coA:diacylglycerol acyltransferase that catalyzes the synthesis of triacylgclyerol, which
is stored in LDs. DGAT-2 is localized to LDs when animals are actively feeding. However,
DGAT-2 is undetectable in starved animals. In contrast, another LD associated protein,
the short-chain dehydrogenase 3 (DHS-3), remains stable under the same condition. Our
obe...[
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Lipid droplets (LDs) are conserved organelles for cellular fat storage. In C.elegans,
numerous LDs can be found in intestinal cells, where fat is primarily stored. Proteomic
studies have identified a large set of LD associated proteins. However, mechanisms
governing the targeting and turnover of these proteins are largely unknown. Our lab has
previously identified DGAT-2 as a LD associated protein in C.elegans. DGAT-2 is an acyl-coA:diacylglycerol acyltransferase that catalyzes the synthesis of triacylgclyerol, which
is stored in LDs. DGAT-2 is localized to LDs when animals are actively feeding. However,
DGAT-2 is undetectable in starved animals. In contrast, another LD associated protein,
the short-chain dehydrogenase 3 (DHS-3), remains stable under the same condition. Our
obervations indicate that there may be differential mechanisms for the turnover of LD
associated proteins.
In this study, I found that the degradation of DGAT-2 under starvation condition is
regulated by the LD assoicated ancient ubiquitous protein 1 (AUP-1) in C. elegans. In
addition, I found that AUP-1 may regulate the turnover of DGAT-2 through its interaction with components of the ERAD pathway. I propose that AUP-1 may recruit
sepcific E2 and E3 enzymes to the LDs surface to ubiquitinate DGAT-2 in starved worms.
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