Topic
Sterol esterification
About: Sterol esterification is a research topic. Over the lifetime, 77 publications have been published within this topic receiving 3979 citations.
Papers published on a yearly basis
Papers
TL;DR: It is speculated that ARGP1 participates in the coenzyme A-dependent acylation of substrate(s) other than cholesterol, and unlike any other member of this multigene family, possesses a predicted diacylglycerol binding motif suggesting that it may perform the last acylations in triglyceride biosynthesis.
430 citations
TL;DR: Using a simple cell-free system, cholesterol itself can serve as an ACAT activator in vitro, in addition to its role as anACAT substrate, which is shown to serve as a physiological regulator of ACAT.
170 citations
TL;DR: Human ACAT expressed in sat1 sat2 mutant cells can catalyze esterification of cholesterol and, to a lesser extent, ergosterol in vitro, but restores ergosteryl oleate formation in vivo to only ∼8% of that catalyzed by yeast ASAT in wild-type cells.
156 citations
TL;DR: The results suggest that the effects of PGE(2) in clearing the scales may be associated with its inhibitory effect on abnormal sterol esterification in the skin of the EFA-deficient rats.
151 citations
TL;DR: The identification of a new DAG acyltransferase gene, DGA2, homologous to the ARE genes of Saccharomyces cerevisiae, and the role and function of all four acyl transferase enzymes involved in the final step of neutral lipid synthesis in this oleaginous yeast is reconsidered.
Abstract: Triacylglycerols (TAG) and steryl esters (SE) are the principal storage lipids in all eukaryotic cells. In yeasts, these storage lipids accumulate within special organelles known as lipid bodies (LB). In the lipid accumulation-oriented metabolism of the oleaginous yeast Yarrowia lipolytica, storage lipids are mostly found in the form of TAG, and only small amounts of SE accumulate. We report here the identification of a new DAG acyltransferase gene, DGA2, homologous to the ARE genes of Saccharomyces cerevisiae. This gene encodes a member of the type 1 acyl-CoA:diacylglycerol acyltransferase family (DGAT1), which has not previously been identified in yeasts, but is commonly found in mammals and plants. Unlike the Are proteins in S. cerevisiae, Dga2p makes a major contribution to TAG synthesis via an acyl-CoA-dependent mechanism and is not involved in SE synthesis. This enzyme appears to affect the size and morphology of LB, suggesting a direct role of storage lipid proteins in LB formation. We report that the Are1p of Y. lipolytica was essential for sterol esterification, as deletion of the encoding gene (ARE1) completely abolished SE synthesis. Unlike its homologs in yeasts, YlARE1 has no DAG acyltransferase activity. We also reconsider the role and function of all four acyltransferase enzymes involved in the final step of neutral lipid synthesis in this oleaginous yeast.
151 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2020 | 1 |
| 2018 | 2 |
| 2015 | 2 |
| 2013 | 1 |
| 2012 | 1 |
| 2010 | 1 |