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    DGKE diacylglycerol kinase epsilon [ Homo sapiens (human) ]

    Gene ID: 8526, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Diacylglycerol kinase-epsilon is S-palmitoylated on cysteine in the cytoplasmic end of its N-terminal transmembrane fragment.

    Diacylglycerol kinase-ε is S-palmitoylated on cysteine in the cytoplasmic end of its N-terminal transmembrane fragment.
    Traczyk G, Hromada-Judycka A, Świątkowska A, Wiśniewska J, Ciesielska A, Kwiatkowska K., Free PMC Article

    01/30/2024
    An intact zinc finger motif of the C1B domain is critical for stability and activity of diacylglycerol kinase-epsilon.

    An intact zinc finger motif of the C1B domain is critical for stability and activity of diacylglycerol kinase-ε.
    Traczyk G, Świątkowska A, Hromada-Judycka A, Janikiewicz J, Kwiatkowska K.

    11/13/2023
    Loss of diacylglycerol kinase epsilon causes thrombotic microangiopathy by impairing endothelial VEGFA signaling.

    Loss of diacylglycerol kinase ε causes thrombotic microangiopathy by impairing endothelial VEGFA signaling.
    Liu D, Ding Q, Dai DF, Padhy B, Nayak MK, Li C, Purvis M, Jin H, Shu C, Chauhan AK, Huang CL, Attanasio M., Free PMC Article

    02/19/2022
    Various phenotypes of disease associated with mutated DGKE gene.

    Various phenotypes of disease associated with mutated DGKE gene.
    Bezdíčka M, Pavlíček P, Bláhová K, Háček J, Zieg J.

    12/26/2020
    mutations can lead to atypical hemolytic uremic syndrome or membranoproliferative glomerulonephritis

    The Phenotypic Spectrum of Nephropathies Associated with Mutations in Diacylglycerol Kinase ε.
    Azukaitis K, Simkova E, Majid MA, Galiano M, Benz K, Amann K, Bockmeyer C, Gajjar R, Meyers KE, Cheong HI, Lange-Sperandio B, Jungraithmayr T, Frémeaux-Bacchi V, Bergmann C, Bereczki C, Miklaszewska M, Csuka D, Prohászka Z, Killen P, Gipson P, Sampson MG, Lemaire M, Schaefer F., Free PMC Article

    10/21/2017
    Letter/Case Report: atypical haemolytic uraemic syndrome in a Japanese patient with DGKE genetic mutations.

    Atypical haemolytic uraemic syndrome in a Japanese patient with DGKE genetic mutations.
    Miyata T, Uchida Y, Ohta T, Urayama K, Yoshida Y, Fujimura Y.

    07/16/2016
    Report DGKE intronic mutations located beyond the exon-intron boundaries in familial hemolytic uremic syndrome.

    Characterization of a New DGKE Intronic Mutation in Genetically Unsolved Cases of Familial Atypical Hemolytic Uremic Syndrome.
    Mele C, Lemaire M, Iatropoulos P, Piras R, Bresin E, Bettoni S, Bick D, Helbling D, Veith R, Valoti E, Donadelli R, Murer L, Neunhäuserer M, Breno M, Frémeaux-Bacchi V, Lifton R, Remuzzi G, Noris M., Free PMC Article

    03/12/2016
    Data suggest that complement dysregulation influences the onset and disease severity in carriers of diacylglycerol kinase-epsilon mutations

    Complement mutations in diacylglycerol kinase-ε-associated atypical hemolytic uremic syndrome.
    Sánchez Chinchilla D, Pinto S, Hoppe B, Adragna M, Lopez L, Justa Roldan ML, Peña A, Lopez Trascasa M, Sánchez-Corral P, Rodríguez de Córdoba S., Free PMC Article

    05/23/2015
    DGKE silencing in resting endothelial cells does not affect complement activation at their surface.

    Loss of DGKε induces endothelial cell activation and death independently of complement activation.
    Bruneau S, Néel M, Roumenina LT, Frimat M, Laurent L, Frémeaux-Bacchi V, Fakhouri F.

    04/25/2015
    Our study expands the clinical phenotypes associated with mutations in DGKE and challenges the benefits of complement blockade treatment in such patients

    Phenotypic expansion of DGKE-associated diseases.
    Westland R, Bodria M, Carrea A, Lata S, Scolari F, Fremeaux-Bacchi V, D'Agati VD, Lifton RP, Gharavi AG, Ghiggeri GM, Sanna-Cherchi S., Free PMC Article

    09/27/2014
    DGKzeta localizes to the nucleus and is considered to regulate nuclear diacylglycerol signaling.[review]

    DGKζ under stress conditions: “to be nuclear or cytoplasmic, that is the question”.
    Goto K, Tanaka T, Nakano T, Okada M, Hozumi Y, Topham MK, Martelli AM.

    09/20/2014
    Fully activating high-density transfected muscarinic receptors (M1Rs) by oxotremorine-M (Oxo-M) leads to similar calcium, DAG, and PKC signals, but PIP2 is depleted.

    Quantitative properties and receptor reserve of the DAG and PKC branch of G(q)-coupled receptor signaling.
    Falkenburger BH, Dickson EJ, Hille B., Free PMC Article

    03/1/2014
    Recessive mutations in DGKE cause atypical hemolytic-uremic syndrome.

    Recessive mutations in DGKE cause atypical hemolytic-uremic syndrome.
    Lemaire M, Frémeaux-Bacchi V, Schaefer F, Choi M, Tang WH, Le Quintrec M, Fakhouri F, Taque S, Nobili F, Martinez F, Ji W, Overton JD, Mane SM, Nürnberg G, Altmüller J, Thiele H, Morin D, Deschenes G, Baudouin V, Llanas B, Collard L, Majid MA, Simkova E, Nürnberg P, Rioux-Leclerc N, Moeckel GW, Gubler MC, Hwa J, Loirat C, Lifton RP., Free PMC Article

    06/22/2013
    Substrate specificity of DGKE is not a consequence of competition with hydrolysis of ATP.

    The basis of the substrate specificity of the epsilon isoform of human diacylglycerol kinase is not a consequence of competing hydrolysis of ATP.
    Prodeus A, Berno B, Topham MK, Epand RM.

    05/11/2013
    performed homozygosity mapping and whole exome sequencing in a Turkish consanguineous family and identified DGKE gene variants as the cause of a membranoproliferative-like glomerular microangiopathy

    DGKE variants cause a glomerular microangiopathy that mimics membranoproliferative GN.
    Ozaltin F, Li B, Rauhauser A, An SW, Soylemezoglu O, Gonul II, Taskiran EZ, Ibsirlioglu T, Korkmaz E, Bilginer Y, Duzova A, Ozen S, Topaloglu R, Besbas N, Ashraf S, Du Y, Liang C, Chen P, Lu D, Vadnagara K, Arbuckle S, Lewis D, Wakeland B, Quigg RJ, Ransom RF, Wakeland EK, Topham MK, Bazan NG, Mohan C, Hildebrandt F, Bakkaloglu A, Huang CL, Attanasio M., Free PMC Article

    04/27/2013
    Inhibition of lipid signaling enzyme diacylglycerol kinase epsilon attenuates mutant huntingtin toxicity.

    Inhibition of lipid signaling enzyme diacylglycerol kinase epsilon attenuates mutant huntingtin toxicity.
    Zhang N, Li B, Al-Ramahi I, Cong X, Held JM, Kim E, Botas J, Gibson BW, Ellerby LM., Free PMC Article

    08/25/2012
    A role for diacylglycerol kinase (DGK) and its downstream product phosphatidic acid (PA) in ANCA-induced neutrophil exocytosis, is reported.

    A dual role for diacylglycerol kinase generated phosphatidic acid in autoantibody-induced neutrophil exocytosis.
    Holden NJ, Savage CO, Young SP, Wakelam MJ, Harper L, Williams JM., Free PMC Article

    08/4/2012
    The region responsible for this arachidonoyl specificity is the lipoxygenase (LOX)-like motif found in the accessory domain, adjacent to DGKvarepsilon's catalytic site.

    Catalytic activity and acyl-chain selectivity of diacylglycerol kinase ɛ are modulated by residues in and near the lipoxygenase-like motif.
    D'Souza K, Epand RM.

    06/16/2012
    diacylglycerol kinase-epsilon (DGKepsilon) has less preference for the acyl chain at the sn-1 position of diacylglycerol (DAG) than the one at the sn-2 position

    Substrate specificity of diacylglycerol kinase-epsilon and the phosphatidylinositol cycle.
    Shulga YV, Topham MK, Epand RM., Free PMC Article

    01/28/2012
    DGK activity is reduced by oxidative stress in human mesangial cells cultured under high glucose conditions.

    Reversal of redox-dependent inhibition of diacylglycerol kinase by antioxidants in mesangial cells exposed to high glucose.
    Atsumi H, Kitada M, Kanasaki K, Koya D.

    11/5/2011
    Data show that Diacylglycerol that 2-arachidonoyl glycerol is a very poor substrate for either the epsilon or the zeta isoforms of diacylglycerol kinases.

    Endocannabinoids and diacylglycerol kinase activity.
    Gantayet A, Jegatheswaran J, Jayakumaran G, Topham MK, Epand RM., Free PMC Article

    07/2/2011
    Substrate specificity of diacylglycerol kinase epsilon is determined by selectivity of the sn-1 and sn-2 acyl chains phosphatidic acid or diacylglycerol.

    Diacylglycerol kinase epsilon is selective for both acyl chains of phosphatidic acid or diacylglycerol.
    Lung M, Shulga YV, Ivanova PT, Myers DS, Milne SB, Brown HA, Topham MK, Epand RM., Free PMC Article

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (2) articles

    The role of height-associated loci identified in genome wide association studies in the determination of pediatric stature.
    Zhao J, Li M, Bradfield JP, Zhang H, Mentch FD, Wang K, Sleiman PM, Kim CE, Glessner JT, Hou C, Keating BJ, Thomas KA, Garris ML, Deliard S, Frackelton EC, Otieno FG, Chiavacci RM, Berkowitz RI, Hakonarson H, Grant SF.

    Phosphoinositide cycle gene polymorphisms affect the plasma lipid profile in the Quebec Family Study.
    Dolley G, Lamarche B, Després JP, Bouchard C, Pérusse L, Vohl MC.

    04/8/2009
    The alpha and zeta isoforms of diacylglycerol kinase are inhibited by 2,3-dioleoylglycerol, but not the more substrate-selective epsilon isoform

    Substrate chirality and specificity of diacylglycerol kinases and the multisubstrate lipid kinase.
    Epand RM, Shulga YV, Timmons HC, Perri AL, Belani JD, Perinpanathan K, Johnson-McIntire LB, Bajjalieh S, Dicu AO, Elias C, Rychnovsky SD, Topham MK.

    01/21/2010
    The hydrophobic domain of diacylglycerol kinase epsilon does not contribute to substrate specificity but plays a role in permanently sequestering the enzyme to a membrane.

    Role of the hydrophobic segment of diacylglycerol kinase epsilon.
    Dicu AO, Topham MK, Ottaway L, Epand RM.

    01/21/2010
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