ArticleThe Journal of biological chemistry2012
Controlling lipid fluxes at glycerol-3-phosphate acyltransferase step in yeast: unique contribution of Gat1p to oleic acid-induced lipid particle formation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
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- Seipin collaborates with the ER membrane to control the sites of lipid droplet formation.Current opinion in cell biology · 2022Review
- Phosphatidic acid biosynthesis in the model organism yeast Saccharomyces cerevisiae - a survey.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021Review
- Reprogramming of fatty acid metabolism in cancer.British journal of cancer · 2020Review
- Tubular ER Associates With Diacylglycerol-Rich Structures During Lipid Droplet Consumption.Frontiers in cell and developmental biology · 2020Article
- Antihyperlipidemic activity ofJournal of food science and technology · 2017Article
- SEIPIN Regulates Lipid Droplet Expansion and Adipocyte Development by Modulating the Activity of Glycerol-3-phosphate Acyltransferase.Cell reports · 2016Article
- Four Acyltransferases Uniquely Contribute to Phospholipid Heterogeneity inLipid insights · 2016Article
- Lipid droplet dynamics in budding yeast.Cellular and molecular life sciences : CMLS · 2015Review
- Tracking Diacylglycerol and Phosphatidic Acid Pools in Budding Yeast.Lipid insights · 2015Review
- Article
- Lipid droplets and peroxisomes: key players in cellular lipid homeostasis or a matter of fat--store 'em up or burn 'em down.Genetics · 2013Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The ability to channel excess fatty acids into neutral lipids like triacylglycerol (TAG) is a critical strategy used by cells to maintain lipid homeostasis. Upon activation to acyl-CoA, fatty acids become readily available as substrates for acyltransferases involved in neutral lipid synthesis. Neutral lipids are then packed into organelles derived from the endoplasmic reticulum called lipid particles (LPs). The first acylation step in the de novo pathway for TAG synthesis is catalyzed by glycerol-3-phosphate acyltransferases (GPATs). Two isoforms, Gat1p/Gpt2p and Gat2p/Sct1p, are present in the yeast Saccharomyces cerevisiae. Previous evidence indicated that these enzymes contribute differentially to the synthesis of TAG in actively growing cells. In this work we studied the role of the yeast GPATs in the formation of LPs induced by a surplus of oleic acid. Yeast lacking Gat1p (but not Gat2p) were sensitive to oleate and failed to accumulate LPs induced by this unsaturated fatty acid. It is shown that oleate induces dephosphorylation of Gat1p as well as an increment in its levels. Most importantly, we identified novel Gat1p crescent structures that are formed in the presence of oleate. These structures are connected with the endoplasmic reticulum and are intimately associated with LPs. No such structures were observed for Gat2p. A crucial point of control of lipid fluxes at the GPAT step is proposed.
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