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Article ; Online: A new method for quantifying the enzyme activity of DGKs.

Barbernitz, Millie Xin / Raben, Daniel M

2023 Volume 91, Page(s) 100998

Abstract: ... relys on a radiometric assay (Epand and Topham, 2007; Tu-Sekine and Raben, 2017). This assay quantifies ...

Abstract	Diacylglycerol kinases (DGKs) are a family of enzymes that catalyze the ATP-dependent conversion of diacylglycerol (DAG) to phosphatidic acid (PtdOH). A common approach to examine the activity of these enzymes relys on a radiometric assay (Epand and Topham, 2007; Tu-Sekine and Raben, 2017). This assay quantifies the DGK-catalyzed incorporation of
MeSH term(s)	Humans ; Diacylglycerol Kinase/genetics ; Diacylglycerol Kinase/metabolism ; Diglycerides/metabolism ; Signal Transduction/physiology
Chemical Substances	Diacylglycerol Kinase (EC 2.7.1.107) ; Diglycerides
Language	English
Publishing date	2023-11-10
Publishing country	England
Document type	Journal Article
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2023.100998
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Article ; Online: Phosphorylation of DGK.

Barbernitz, Xin / Raben, Daniel M

Advances in biological regulation

2022 Volume 88, Page(s) 100941

Abstract: Diacylglycerol (DAG) and phosphatidic acid (PtdOH) play important roles in a variety of signaling cascades (Carrasco and Merida, 2007; Stace and Ktistakis, 2006). Therefore, the physiological roles and regulatory mechanisms controlling the levels of ... ...

Abstract	Diacylglycerol (DAG) and phosphatidic acid (PtdOH) play important roles in a variety of signaling cascades (Carrasco and Merida, 2007; Stace and Ktistakis, 2006). Therefore, the physiological roles and regulatory mechanisms controlling the levels of these lipids are important. One class of enzymes capable of coordinating the levels of these two lipids are the diacylglycerol kinases (DGKs). DGKs catalyze the transfer of the γ-phosphate of ATP to the hydroxyl group of DAG which generates PtdOH(Merida et al., 2008; Sakane et al., 2007). As DGKs reciprocally modulate the relative levels of these two signaling lipids, it is not surprising that there is increasing interest in understanding the mechanism underlying the catalysis and regulation of these kinases. While post-translational modifications (PTMs) are often involved in enzyme regulation, there is surprisingly little information regarding the PTMs on these enzymes and their roles in modulating their activity and function. In this review, we will summarize what is known about one PTM on DGKs, phosphorylation, and the possible functions of this modification.
MeSH term(s)	Humans ; Diglycerides ; Phosphorylation ; Diacylglycerol Kinase/genetics ; Diacylglycerol Kinase/metabolism
Chemical Substances	Diglycerides ; Diacylglycerol Kinase (EC 2.7.1.107)
Language	English
Publishing date	2022-12-07
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2022.100941
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Article ; Online: The role of N-terminal phosphorylation of DGK-θ.

Barbernitz, Millie X / Devine, Lauren R / Cole, Robert N / Raben, Daniel M

Journal of lipid research

2024 Volume 65, Issue 3, Page(s) 100506

Abstract: Diacylglycerol kinases (DGKs) are lipid kinases that mediate the phosphorylation of diacylglycerol (DAG) leading to the production of phosphatidic acid (PtdOH). To examine the role of phosphorylation on DGK-θ, we first identified the phosphorylated sites ...

Abstract	Diacylglycerol kinases (DGKs) are lipid kinases that mediate the phosphorylation of diacylglycerol (DAG) leading to the production of phosphatidic acid (PtdOH). To examine the role of phosphorylation on DGK-θ, we first identified the phosphorylated sites on endogenous DGK-θ from mouse brain and found four sites: S15, S17, which we refer to phosphomotif-1 sites, and S22 and S26 which we refer to as phosphomotif-2 sites. This study focused on the role of these phosphorylated sites on enzyme activity, membrane binding, thermal stability, and cellular half-life of DGK-θ. After generating a construct devoid of all non-catalytic phosphorylation sites (4A), we also generated other constructs to mimic phosphorylation of these residues by mutating them to glutamate (E). Our data demonstrate that an increase in membrane affinity requires the phosphorylation of all four endogenous sites as the phosphomimetic 4E but not other phosphomimietics. Furthermore, 4E also shows an increase in basal activity as well as an increase in the Syt1-induced activity compared to 4A. It is noteworthy that these phosphorylations had no effect on the thermal stability or cellular half-life of this enzyme. Interestingly, when only one phosphorylation domain (phosphomotif-1 or phosphomotif-2) contained phosphomimetics (S15E/S17E or S22E/S26E), the basal activity was also increased but membrane binding affinity was not increased. Furthermore, when only one residue in each domain mimicked an endogenous phosphorylated serine (S15E/S22E or S17E/S26E), the Syt1-induced activity as well as membrane binding affinity decreased relative to 4A. These results indicate that these endogenous phosphorylation sites contribute differentially to membrane binding and enzymatic activity.
MeSH term(s)	Animals ; Mice ; Phosphorylation ; Diglycerides/metabolism ; Diacylglycerol Kinase/genetics ; Diacylglycerol Kinase/metabolism
Chemical Substances	Diglycerides ; Diacylglycerol Kinase (EC 2.7.1.107)
Language	English
Publishing date	2024-01-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1016/j.jlr.2024.100506
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Article: Lipid Metabolism Crosstalk in the Brain: Glia and Neurons.

Barber, Casey N / Raben, Daniel M

Frontiers in cellular neuroscience

2019 Volume 13, Page(s) 212

Abstract: Until recently, glial cells have been considered mainly support cells for neurons in the mammalian brain. However, many studies have unveiled a variety of glial functions including electrolyte homeostasis, inflammation, synapse formation, metabolism, and ...

Abstract	Until recently, glial cells have been considered mainly support cells for neurons in the mammalian brain. However, many studies have unveiled a variety of glial functions including electrolyte homeostasis, inflammation, synapse formation, metabolism, and the regulation of neurotransmission. The importance of these functions illuminates significant crosstalk between glial and neuronal cells. Importantly, it is known that astrocytes secrete signals that can modulate both presynaptic and postsynaptic function. It is also known that the lipid compositions of the pre- and post-synaptic membranes of neurons greatly impact functions such as vesicle fusion and receptor mobility. These data suggest an essential lipid-mediated communication between glial cells and neurons. Little is known, however, about how the lipid metabolism of both cell types may interact. In this review, we discuss neuronal and glial lipid metabolism and suggest how they might interact to impact neurotransmission.
Language	English
Publishing date	2019-05-21
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2019.00212
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Article ; Online: Roles of DGKs in neurons: Postsynaptic functions?

Barber, Casey N / Raben, Daniel M

Advances in biological regulation

2019 Volume 75, Page(s) 100688

Abstract: Diacylglycerol kinases (DGKs) contribute to an important part of intracellular signaling because, in addition to reducing diacylglycerol levels, they generate phosphatidic acid (PtdOH) Recent research has led to the discovery of ten mammalian DGK ... ...

Abstract	Diacylglycerol kinases (DGKs) contribute to an important part of intracellular signaling because, in addition to reducing diacylglycerol levels, they generate phosphatidic acid (PtdOH) Recent research has led to the discovery of ten mammalian DGK isoforms, all of which are found in the mammalian brain. Many of these isoforms have studied functions within the brain, while others lack such understanding in regards to neuronal roles, regulation, and structural dynamics. However, while previously a neuronal function for DGKθ was unknown, it was recently found that DGKθ is required for the regulation of synaptic vesicle endocytosis and work is currently being conducted to elucidate the mechanism behind this regulation. Here we will review some of the roles of all mammalian DGKs and hypothesize additional roles. We will address the topic of redundancy among the ten DGK isoforms and discuss the possibility that DGKθ, among other DGKs, may have unstudied postsynaptic functions. We also hypothesize that in addition to DGKθ's presynaptic endocytic role, DGKθ might also regulate the endocytosis of AMPA receptors and other postsynaptic membrane proteins.
MeSH term(s)	Animals ; Diacylglycerol Kinase/genetics ; Diacylglycerol Kinase/metabolism ; Endocytosis ; Humans ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Mice ; Neurons/enzymology ; Phosphatidic Acids/genetics ; Phosphatidic Acids/metabolism ; Receptors, AMPA/genetics ; Receptors, AMPA/metabolism ; Synaptic Membranes/enzymology ; Synaptic Membranes/genetics ; Synaptic Vesicles/enzymology ; Synaptic Vesicles/genetics
Chemical Substances	Isoenzymes ; Phosphatidic Acids ; Receptors, AMPA ; Diacylglycerol Kinase (EC 2.7.1.107)
Language	English
Publishing date	2019-11-28
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2019.100688
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Article ; Online: Elusive structure of mammalian DGKs.

Ma, Qianqian / Srinivasan, Lakshmi / Gabelli, Sandra B / Raben, Daniel M

Advances in biological regulation

2021 Volume 83, Page(s) 100847

Abstract: Mammalian diacylglycerol kinases (DGKs) are a group of enzymes that catalyze the ATP-dependent phosphorylation of diacylglycerol (DAG) to produce phosphatidic acid (PtdOH). In doing so, they modulate the levels of these two important signaling lipids. ... ...

Abstract	Mammalian diacylglycerol kinases (DGKs) are a group of enzymes that catalyze the ATP-dependent phosphorylation of diacylglycerol (DAG) to produce phosphatidic acid (PtdOH). In doing so, they modulate the levels of these two important signaling lipids. Currently, ten mammalian DGKs are organized into five classes that vary with respect to domain organization, regulation, and cellular/subcellular distribution. As lipids play critical roles in cells, it is not surprising that there is increasing interest in understanding the mechanism underlying the catalysis and regulation of lipid modulating enzymes such as DGKs. However, there are no solved 3D structures for any of the eukaryotic DGKs. In this review, we summarize what is known and the current challenges in determining the structures of these important enzymes. In addition to gain critical insights into their mechanisms of catalysis and regulation, DGK structures will provide a platform for the design of isoform specific inhibitors.
MeSH term(s)	Animals ; Diacylglycerol Kinase/metabolism ; Humans ; Mammals/genetics ; Mammals/metabolism ; Phosphatidic Acids ; Phosphorylation ; Protein Isoforms ; Signal Transduction
Chemical Substances	Phosphatidic Acids ; Protein Isoforms ; Diacylglycerol Kinase (EC 2.7.1.107)
Language	English
Publishing date	2021-12-02
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2021.100847
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Article ; Online: Phosphatidic acid and neurotransmission.

Raben, Daniel M / Barber, Casey N

Advances in biological regulation

2017 Volume 63, Page(s) 15–21

Abstract: Lipids play a vital role in the health and functioning of neurons and interest in the physiological role of neuronal lipids is certainly increasing. One neuronal function in which neuronal lipids appears to play key roles in neurotransmission. Our ... ...

Abstract	Lipids play a vital role in the health and functioning of neurons and interest in the physiological role of neuronal lipids is certainly increasing. One neuronal function in which neuronal lipids appears to play key roles in neurotransmission. Our understanding of the role of lipids in the synaptic vesicle cycle and neurotransmitter release is becoming increasingly more important. Much of the initial research in this area has highlighted the major roles played by the phosphoinositides (PtdIns), diacylglycerol (DAG), and phosphatidic acid (PtdOH). Of these, PtdOH has not received as much attention as the other lipids although its role and metabolism appears to be extremely important. This lipid has been shown to play a role in modulating both exocytosis and endocytosis although its precise role in either process is not well defined. The currently evidence suggest this lipid likely participates in key processes by altering membrane architecture necessary for membrane fusion, mediating the penetration of membrane proteins, serving as a precursor for other important SV cycling lipids, or activating essential enzymes. In this review, we address the sources of PtdOH, the enzymes involved in its production, the regulation of these enzymes, and its potential roles in neurotransmission in the central nervous system.
Language	English
Publishing date	2017-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2016.09.004
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Article ; Online: Differential expression patterns of phospholipase D isoforms 1 and 2 in the mammalian brain and retina.

Barber, Casey N / Goldschmidt, Hana L / Lilley, Brendan / Bygrave, Alexei M / Johnson, Richard C / Huganir, Richard L / Zack, Donald J / Raben, Daniel M

Journal of lipid research

2022 Volume 63, Issue 8, Page(s) 100247

Abstract: Phosphatidic acid is a key signaling molecule heavily implicated in exocytosis due to its protein-binding partners and propensity to induce negative membrane curvature. One phosphatidic acid-producing enzyme, phospholipase D (PLD), has also been ... ...

Abstract	Phosphatidic acid is a key signaling molecule heavily implicated in exocytosis due to its protein-binding partners and propensity to induce negative membrane curvature. One phosphatidic acid-producing enzyme, phospholipase D (PLD), has also been implicated in neurotransmission. Unfortunately, due to the unreliability of reagents, there has been confusion in the literature regarding the expression of PLD isoforms in the mammalian brain which has hampered our understanding of their functional roles in neurons. To address this, we generated epitope-tagged PLD1 and PLD2 knockin mice using CRISPR/Cas9. Using these mice, we show that PLD1 and PLD2 are both localized at synapses by adulthood, with PLD2 expression being considerably higher in glial cells and PLD1 expression predominating in neurons. Interestingly, we observed that only PLD1 is expressed in the mouse retina, where it is found in the synaptic plexiform layers. These data provide critical information regarding the localization and potential role of PLDs in the central nervous system.
MeSH term(s)	Animals ; Brain ; Mice ; Phosphatidic Acids ; Phospholipase D ; Protein Isoforms ; Retina
Chemical Substances	Phosphatidic Acids ; Protein Isoforms ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2022-06-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80154-9
ISSN	1539-7262 ; 0022-2275
ISSN (online)	1539-7262
ISSN	0022-2275
DOI	10.1016/j.jlr.2022.100247
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Article: Identification of Synaptic DGKθ Interactors That Stimulate DGKθ Activity.

Barber, Casey N / Goldschmidt, Hana L / Ma, Qianqian / Devine, Lauren R / Cole, Robert N / Huganir, Richard L / Raben, Daniel M

Frontiers in synaptic neuroscience

2022 Volume 14, Page(s) 855673

Abstract: Lipids and their metabolic enzymes are a critical point of regulation for the membrane curvature required to induce membrane fusion during synaptic vesicle recycling. One such enzyme is diacylglycerol kinase θ (DGKθ), which produces phosphatidic acid ( ... ...

Abstract	Lipids and their metabolic enzymes are a critical point of regulation for the membrane curvature required to induce membrane fusion during synaptic vesicle recycling. One such enzyme is diacylglycerol kinase θ (DGKθ), which produces phosphatidic acid (PtdOH) that generates negative membrane curvature. Synapses lacking DGKθ have significantly slower rates of endocytosis, implicating DGKθ as an endocytic regulator. Importantly, DGKθ kinase activity is required for this function. However, protein regulators of DGKθ's kinase activity in neurons have never been identified. In this study, we employed APEX2 proximity labeling and mass spectrometry to identify endogenous interactors of DGKθ in neurons and assayed their ability to modulate its kinase activity. Seven endogenous DGKθ interactors were identified and notably, synaptotagmin-1 (Syt1) increased DGKθ kinase activity 10-fold. This study is the first to validate endogenous DGKθ interactors at the mammalian synapse and suggests a coordinated role between DGKθ-produced PtdOH and Syt1 in synaptic vesicle recycling.
Language	English
Publishing date	2022-04-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2592086-8
ISSN	1663-3563
ISSN	1663-3563
DOI	10.3389/fnsyn.2022.855673
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Article ; Online: Diacylglycerol kinases: Relationship to other lipid kinases.

Ma, Qianqian / Gabelli, Sandra B / Raben, Daniel M

Advances in biological regulation

2018 Volume 71, Page(s) 104–110

Abstract: Lipid kinases regulate a wide variety of cellular functions and have emerged as one the most promising targets for drug design. Diacylglycerol kinases (DGKs) are a family of enzymes that catalyze the ATP-dependent phosphorylation of diacylglycerol (DAG) ... ...

Abstract	Lipid kinases regulate a wide variety of cellular functions and have emerged as one the most promising targets for drug design. Diacylglycerol kinases (DGKs) are a family of enzymes that catalyze the ATP-dependent phosphorylation of diacylglycerol (DAG) to phosphatidic acid (PtdOH). Despite the critical role in lipid biosynthesis, both DAG and PtdOH have been shown as bioactive lipids mediating a number of signaling pathways. Although there is increasing recognition of their role in signaling systems, our understanding of the key enzyme which regulate the balance of these two lipid messages remain limited. Solved structures provide a wealth of information for understanding the function and regulation of these enzymes. Solving the structures of mammalian DGKs by traditional NMR and X-ray crystallography approaches have been challenging and so far, there are still no three-dimensional structures of these DGKs. Despite this, some insights may be gained by examining the similarities and differences between prokaryotic DGKs and other mammalian lipid kinases. This review focuses on summarizing and comparing the structure of prokaryotic and mammalian DGKs as well as two other lipid kinases: sphingosine kinase and phosphatidylinositol-3-kinase. How these known lipid kinases structures relate to mammalian DGKs will also be discussed.
MeSH term(s)	Animals ; Crystallography, X-Ray ; Diacylglycerol Kinase/chemistry ; Diacylglycerol Kinase/genetics ; Diacylglycerol Kinase/metabolism ; Diglycerides/chemistry ; Diglycerides/genetics ; Diglycerides/metabolism ; Humans ; Phosphatidic Acids/chemistry ; Phosphatidic Acids/genetics ; Phosphatidic Acids/metabolism ; Phosphorylation ; Protein Domains ; Signal Transduction
Chemical Substances	1,2-diacylglycerol ; Diglycerides ; Phosphatidic Acids ; Diacylglycerol Kinase (EC 2.7.1.107)
Language	English
Publishing date	2018-09-28
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2018.09.014
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