ArticleThe Journal of biological chemistry2012
Dual regulation of diacylglycerol kinase (DGK)-θ: polybasic proteins promote activation by phospholipids and increase substrate affinity.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Identification of Synaptic DGKθ Interactors That Stimulate DGKθ Activity.Frontiers in synaptic neuroscience · 2022Article
- Elusive structure of mammalian DGKs.Advances in biological regulation · 2022Review
- Increasing kinase domain proximity promotes MST2 autophosphorylation during Hippo signaling.The Journal of biological chemistry · 2020Article
- Beyond Lipid Signaling: Pleiotropic Effects of Diacylglycerol Kinases in Cellular Signaling.International journal of molecular sciences · 2020Review
- Diacylglycerol kinases: Relationship to other lipid kinases.Advances in biological regulation · 2019Review
- The SUMO-specific isopeptidase SENP2 is targeted to intracellular membranes via a predicted N-terminal amphipathic α-helix.Molecular biology of the cell · 2018Article
- Phosphatidic acid and neurotransmission.Advances in biological regulation · 2017Review
- DGKθ Catalytic Activity Is Required for Efficient Recycling of Presynaptic Vesicles at Excitatory Synapses.Cell reports · 2016Article
- Phosphatidylserine in the brain: metabolism and function.Progress in lipid research · 2014Review
- The expression of diacylglycerol kinase theta during the organogenesis of mouse embryos.BMC developmental biology · 2013Article
- Diacylglycerol kinase θ couples farnesoid X receptor-dependent bile acid signalling to Akt activation and glucose homoeostasis in hepatocytes.The Biochemical journal · 2013Article
- Bacterial expression strategies for several Sus scrofa diacylglycerol kinase alpha constructs: solubility challenges.Scientific reports · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Diacylglycerol kinases are important mediators of lipid signaling cascades, and insight into their regulation is of increasing interest. Using purified DGK-θ, we show that this isoform is subject to dual regulation and that the previously characterized stimulation by acidic phospholipids is dependent on the presence of a positively charged protein or peptide. Polybasic cofactors lowered the K(m) for diacylglycerol at the membrane surface (K(m)((surf))), and worked synergistically with acidic phospholipids to increase activity 10- to 30-fold, suggesting that the purified enzyme is autoinhibited. Vesicle pulldown studies showed that acidic phospholipids recruit polybasic cofactors to the vesicle surface but have little effect on the membrane association of DGK-θ, suggesting that a triad of enzyme, acidic lipid and basic protein are necessary for interfacial activity. Importantly, these data demonstrate that the interfacial association and catalytic activity of DGK-θ are independently regulated. Finally, we show that DGK-θ directly interacts with, and is activated by, basic proteins such as histone H1 and Tau with nm affinity, consistent with a potential role for a polybasic protein or protein domain in the activation of this enzyme.
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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 OpenQuestion graph.