ArticleThe Journal of biological chemistry2009
Diacylglycerol kinase epsilon is selective for both acyl chains of phosphatidic acid or diacylglycerol.
Article in The Journal of biological chemistry, 2009. 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, 67 citations in OpenAlex.
- Diacylglycerol kinase-ε is required for the formation of GPI-anchored CD14 and the LPS-induced proinflammatory responses of macrophages.Cell communication and signaling : CCS · 2026Article
- DGKs in lipid signaling and disease intervention: structural basis, pathological mechanisms, and emerging therapeutic strategies.Cellular & molecular biology letters · 2025Review
- Father's adolescent body silhouette is associated with offspring asthma, lung function and BMI through DNA methylation.Communications biology · 2025Article
- Diacylglycerol Kinases and Its Role in Lipid Metabolism and Related Diseases.International journal of molecular sciences · 2024Review
- Acyl chain selection couples the consumption and synthesis of phosphoinositides.The EMBO journal · 2022Article
- Article
- Phosphoinositides signaling modulates microglial actin remodeling and phagocytosis in Alzheimer's disease.Cell communication and signaling : CCS · 2021Review
- Diacylglycerol kinases regulate TRPV1 channel activity.The Journal of biological chemistry · 2020Article
- Regulation of DGKε Activity and Substrate Acyl Chain Specificity by Negatively Charged Phospholipids.Biophysical journal · 2020Article
- Reprogramming fatty acyl specificity of lipid kinases via C1 domain engineering.Nature chemical biology · 2020Article
- CDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis.Frontiers in cell and developmental biology · 2020Review
- How is the acyl chain composition of phosphoinositides created and does it matter?Biochemical Society transactions · 2019Review
- Diacylglycerol kinases: Relationship to other lipid kinases.Advances in biological regulation · 2019Review
- Features of the Phosphatidylinositol Cycle and its Role in Signal Transduction.The Journal of membrane biology · 2017Review
- Diacylglycerol kinase ε deficiency preserves glucose tolerance and modulates lipid metabolism in obese mice.Journal of lipid research · 2017Article
- Decreased 16:0/20:4-phosphatidylinositol level in the post-mortem prefrontal cortex of elderly patients with schizophrenia.Scientific reports · 2017Article
- Dual activities of ritanserin and R59022 as DGKα inhibitors and serotonin receptor antagonists.Biochemical pharmacology · 2017Article
- Four Acyltransferases Uniquely Contribute to Phospholipid Heterogeneity inLipid insights · 2016Article
- Diacylglycerol Kinase-ε: Properties and Biological Roles.Frontiers in cell and developmental biology · 2016Review
- DAG tales: the multiple faces of diacylglycerol--stereochemistry, metabolism, and signaling.Cellular and molecular life sciences : CMLS · 2015Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The phosphatidylinositol (PI) cycle mediates many cellular events by controlling the metabolism of many lipid second messengers. Diacylglycerol kinase epsilon (DGK epsilon) has an important role in this cycle. DGK epsilon is the only DGK isoform to show inhibition by its product phosphatidic acid (PA) as well as substrate specificity for sn-2 arachidonoyl-diacylglycerol (DAG). Here, we show that this inhibition and substrate specificity are both determined by selectivity for a combination of the sn-1 and sn-2 acyl chains of PA or DAG, respectively, preferring the most prevalent acyl chain composition of lipids involved specifically in the PI cycle, 1-stearoyl-2-arachidonoyl. Although the difference in rate for closely related lipid species is small, there is a significant enrichment of 1-stearoyl-2-arachidonoyl PI because of the cyclical nature of PI turnover. We also show that the inhibition of DGK epsilon by PA is competitive and that the deletion of the hydrophobic segment and cationic cluster of DGK epsilon does not affect its selectivity for the acyl chains of PA or DAG. Thus, this active site not only recognizes the lipid headgroup but also a combination of the two acyl chains in PA or DAG. We propose a mechanism of DGK epsilon regulation where its dual acyl chain selectivity is used to negatively regulate its enzymatic activity in a manner that ensures DGK epsilon remains committed to the PI turnover cycle. This novel mechanism of enzyme regulation within a signaling pathway could serve as a template for the regulation of enzymes in other pathways in the cell.
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Registered trials
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 Socratic graph.