ArticleThe Journal of biological chemistry2011
Evidence that diacylglycerol acyltransferase 1 (DGAT1) has dual membrane topology in the endoplasmic reticulum of HepG2 cells.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 68 citations in OpenAlex.
- Infection-specific long-chain fatty acid metabolism as a broad anti-enterovirus target.bioRxiv : the preprint server for biology · 2026Article
- Synergistic mechanisms of DGAT and PDAT in shaping triacylglycerol diversity: evolutionary insights and metabolic engineering strategies.Frontiers in plant science · 2025Review
- Zebrafish are resilient to the loss of major diacylglycerol acyltransferase enzymes.The Journal of biological chemistry · 2024Article
- Spf1 and Ste24: quality controllers of transmembrane protein topology in the eukaryotic cell.Frontiers in cell and developmental biology · 2023Review
- A negative-solvatochromic fluorescent probe for visualizing intracellular distributions of fatty acid metabolites.Nature communications · 2022Article
- An alternative angiosperm DGAT1 topology and potential motifs in the N-terminus.Frontiers in plant science · 2022Article
- Dual topology of co-chaperones at the membrane of the endoplasmic reticulum.Cell death discovery · 2021Review
- The triglyceride synthesis enzymes DGAT1 and DGAT2 have distinct and overlapping functions in adipocytes.Journal of lipid research · 2019Article
- HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit.Cells · 2019Review
- Symposium review: Intravital imaging of the lactating mammary gland in live mice reveals novel aspects of milk-lipid secretion.Journal of dairy science · 2019Article
- Hepatic VLDL secretion: DGAT1 determines particle size but not particle number, which can be supported entirely by DGAT2.Journal of lipid research · 2019Article
- How lipid droplets "TAG" along: Glycerolipid synthetic enzymes and lipid storage.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Dgat1 and Dgat2 regulate enterocyte triacylglycerol distribution and alter proteins associated with cytoplasmic lipid droplets in response to dietary fat.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Article
- Novel Interconnections in Lipid Metabolism Revealed by Overexpression of Sphingomyelin Synthase-1.The Journal of biological chemistry · 2017Article
- Diacylglycerol acyltransferase 2 links glucose utilization to fatty acid oxidation in the brown adipocytes.Journal of lipid research · 2017Article
- Prolonged silencing of diacylglycerol acyltransferase-1 induces a dedifferentiated phenotype in human liver cells.Journal of cellular and molecular medicine · 2016Article
- DAG tales: the multiple faces of diacylglycerol--stereochemistry, metabolism, and signaling.Cellular and molecular life sciences : CMLS · 2015Review
- Type 1 diacylglycerol acyltransferases of Brassica napus preferentially incorporate oleic acid into triacylglycerol.Journal of experimental botany · 2015Article
- Asymmetrical diacylglycerol dynamics on the cytosolic and lumenal sides of a single endomembrane in living cells.Scientific reports · 2015Article
- DGAT1-deficiency affects the cellular distribution of hepatic retinoid and attenuates the progression of CCl4-induced liver fibrosis.Hepatobiliary surgery and nutrition · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Triacylglycerol (TAG) synthesis and secretion are important functions of the liver that have major impacts on health, as overaccumulation of TAG within the liver (steatosis) or hypersecretion of TAG within very low density lipoproteins (VLDL) both have deleterious metabolic consequences. Two diacylglycerol acyltransferases (DGATs 1 and 2) can catalyze the final step in the synthesis of TAG from diacylglycerol, which has been suggested to play an important role in the transfer of the glyceride moiety across the endoplasmic reticular membrane for (re)synthesis of TAG on the lumenal aspect of the endoplasmic reticular (ER) membrane (Owen, M., Corstorphine, C. C., and Zammit, V. A. (1997) Biochem. J. 323, 17-21). Recent topographical studies suggested that the oligomeric enzyme DGAT1 is exclusively lumen facing (latent) in the ER membrane. By contrast, in the present study, using two specific inhibitors of human DGAT1, we present evidence that DGAT1 has a dual topology within the ER of HepG2 cells, with approximately equal DGAT1 activities exposed on the cytosolic and lumenal aspects of the ER membrane. This was confirmed by the observation of the loss of both overt (partial) and latent (total) DGAT activity in microsomes prepared from livers of Dgat1(-/-) mice. Conformational differences between DGAT1 molecules having the different topologies were indicated by the markedly disparate sensitivities of the overt DGAT1 to one of the inhibitors. These data suggest that DGAT1 belongs to the family of oligomeric membrane proteins that adopt a dual membrane topology.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.