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    DGAT2 diacylglycerol O-acyltransferase 2 [ Homo sapiens (human) ]

    Gene ID: 84649, updated on 3-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    DGAT2 stability is increased in response to DGAT1 inhibition in gene edited HepG2 cells.

    DGAT2 stability is increased in response to DGAT1 inhibition in gene edited HepG2 cells.
    McFie PJ, Chumala P, Katselis GS, Stone SJ.

    08/26/2024
    Diurnal expression of Dgat2 induced by time-restricted feeding maintains cardiac health in the Drosophila model of circadian disruption.

    Diurnal expression of Dgat2 induced by time-restricted feeding maintains cardiac health in the Drosophila model of circadian disruption.
    Guo Y, Abou Daya F, Le HD, Panda S, Melkani GC., Free PMC Article

    08/6/2024
    The role of DGAT1 and DGAT2 in regulating tumor cell growth and their potential clinical implications.

    The role of DGAT1 and DGAT2 in regulating tumor cell growth and their potential clinical implications.
    Deng B, Kong W, Shen X, Han C, Zhao Z, Chen S, Zhou C, Bae-Jump V., Free PMC Article

    03/20/2024
    The roles of DGAT1 and DGAT2 in human myotubes are dependent on donor patho-physiological background.

    The roles of DGAT1 and DGAT2 in human myotubes are dependent on donor patho-physiological background.
    Irshad Z, Lund J, Sillars A, Løvsletten NG, Gharanei S, Salt IP, Freeman DJ, Gill JMR, Thoresen GH, Rustan AC, Zammit VA., Free PMC Article

    10/24/2023
    Preferential lipolysis of DGAT1 over DGAT2 generated triacylglycerol in Huh7 hepatocytes.

    Preferential lipolysis of DGAT1 over DGAT2 generated triacylglycerol in Huh7 hepatocytes.
    Selvaraj R, Zehnder SV, Watts R, Lian J, Das C, Nelson R, Lehner R.

    09/12/2023
    DGAT2 Inhibition Potentiates Lipid Droplet Formation To Reduce Cytotoxicity in APOL1 Kidney Risk Variants.

    DGAT2 Inhibition Potentiates Lipid Droplet Formation To Reduce Cytotoxicity in APOL1 Kidney Risk Variants.
    Chun J, Riella CV, Chung H, Shah SS, Wang M, Magraner JM, Ribas GT, Ribas HT, Zhang JY, Alper SL, Friedman DJ, Pollak MR., Free PMC Article

    05/7/2022
    ACC inhibitor alone or co-administered with a DGAT2 inhibitor in patients with non-alcoholic fatty liver disease: two parallel, placebo-controlled, randomized phase 2a trials.

    ACC inhibitor alone or co-administered with a DGAT2 inhibitor in patients with non-alcoholic fatty liver disease: two parallel, placebo-controlled, randomized phase 2a trials.
    Calle RA, Amin NB, Carvajal-Gonzalez S, Ross TT, Bergman A, Aggarwal S, Crowley C, Rinaldi A, Mancuso J, Aggarwal N, Somayaji V, Inglot M, Tuthill TA, Kou K, Boucher M, Tesz G, Dullea R, Bence KK, Kim AM, Pfefferkorn JA, Esler WP.

    11/13/2021
    Obesity promotes gastric cancer metastasis via diacylglycerol acyltransferase 2-dependent lipid droplets accumulation and redox homeostasis.

    Obesity promotes gastric cancer metastasis via diacylglycerol acyltransferase 2-dependent lipid droplets accumulation and redox homeostasis.
    Li S, Wu T, Lu YX, Wang JX, Yu FH, Yang MZ, Huang YJ, Li ZJ, Wang SL, Huang L, Lu L, Tian T., Free PMC Article

    08/7/2021
    These data suggest that Dgat2 is an important regulator of HCC cell proliferation.

    Dgat2 reduces hepatocellular carcinoma malignancy via downregulation of cell cycle-related gene expression.
    Li Y, Li T, Jin Y, Shen J.

    01/18/2020
    A binding assay utilizing (125)I-labeled imidazopyridine demonstrated that the level of imidazopyridine binding to DGAT2 mutant enzymes, H161A and H163A, dramatically decreased to 11-17% of that of the wild-type enzyme, indicating that these residues are critical for imidazopyridines to bind to DGAT2.

    Mechanistic Characterization of Long Residence Time Inhibitors of Diacylglycerol Acyltransferase 2 (DGAT2).
    Pabst B, Futatsugi K, Li Q, Ahn K.

    08/3/2019
    DGAT2 contains a C-terminal signal sequence that interacts with lipid droplets.

    Diacylglycerol acyltransferase-2 contains a c-terminal sequence that interacts with lipid droplets.
    McFie PJ, Banman SL, Stone SJ.

    12/1/2018
    Study identified a large cohort of patients with congenital diarrheal disorders with mutations in DGAT1 that reduced expression of its product; dermal fibroblasts and intestinal organoids derived from these patients had altered lipid metabolism and were susceptible to lipid-induced cell death. Expression of full-length wildtype DGAT1 or DGAT2 restored normal lipid metabolism in these cells.

    Intestinal Failure and Aberrant Lipid Metabolism in Patients With DGAT1 Deficiency.
    van Rijn JM, Ardy RC, Kuloğlu Z, Härter B, van Haaften-Visser DY, van der Doef HPJ, van Hoesel M, Kansu A, van Vugt AHM, Thian M, Kokke FTM, Krolo A, Başaran MK, Kaya NG, Aksu AÜ, Dalgıç B, Ozcay F, Baris Z, Kain R, Stigter ECA, Lichtenbelt KD, Massink MPG, Duran KJ, Verheij JBGM, Lugtenberg D, Nikkels PGJ, Brouwer HGF, Verkade HJ, Scheenstra R, Spee B, Nieuwenhuis EES, Coffer PJ, Janecke AR, van Haaften G, Houwen RHJ, Müller T, Middendorp S, Boztug K., Free PMC Article

    08/25/2018
    We first report loss-of-function mutations in DGAT2 and FAAH in one obese subject, which may interact with each other to affect the adiposity penetrance, providing a model of genetic interaction associated with human obesity.

    Genetic interaction of DGAT2 and FAAH in the development of human obesity.
    Ning T, Zou Y, Yang M, Lu Q, Chen M, Liu W, Zhao S, Sun Y, Shi J, Ma Q, Hong J, Liu R, Wang J, Ning G.

    09/30/2017
    The findings indicate the functionality of the prostate cancer death-predisposing SNPs rs143975731, rs12277366, rs2155225, and rs2155222 as DGAT2 regulators in prostate tumors.

    Expressional profiling of prostate cancer risk SNPs at 11q13.5 identifies DGAT2 as a new target gene.
    Nurminen R, Rantapero T, Wong SC, Fischer D, Lehtonen R, Tammela TL, Nykter M, Visakorpi T, Wahlfors T, Schleutker J.

    07/8/2017
    Diacylglycerol acyltransferase-2 and monoacylglycerol acyltransferase-2 are ubiquitinated proteins that are degraded by the 26S proteasome

    Diacylglycerol acyltransferase-2 and monoacylglycerol acyltransferase-2 are ubiquitinated proteins that are degraded by the 26S proteasome.
    Brandt C, McFie PJ, Stone SJ.

    06/24/2017
    Results identified a novel de novo p.Y223H mutation in the DGAT2 from an autosomal-dominant Korean Charcot-Marie-Tooth (CMT) family suggesting this mutation a novel underlying cause of an autosomal-dominant CMT2 phenotype.

    DGAT2 Mutation in a Family with Autosomal-Dominant Early-Onset Axonal Charcot-Marie-Tooth Disease.
    Hong YB, Kang J, Kim JH, Lee J, Kwak G, Hyun YS, Nam SH, Hong HD, Choi YR, Jung SC, Koo H, Lee JE, Choi BO, Chung KW.

    12/31/2016
    uPA/uPAR stimulates triglyceride synthesis in Huh7 hepatoma cells via p38-dependent upregulation of DGAT2

    Urokinase-type plasminogen activator (uPA) stimulates triglyceride synthesis in Huh7 hepatoma cells via p38-dependent upregulation of DGAT2.
    Paland N, Gamliel-Lazarovich A, Coleman R, Fuhrman B.

    08/22/2015
    DGAT2 is regulated by gp78-associated endoplasmic-reticulum-associated degradation at the post-translational level.

    Regulation of diacylglycerol acyltransferase 2 protein stability by gp78-associated endoplasmic-reticulum-associated degradation.
    Choi K, Kim H, Kang H, Lee SY, Lee SJ, Back SH, Lee SH, Kim MS, Lee JE, Park JY, Kim J, Kim S, Song JH, Choi Y, Lee S, Lee HJ, Kim JH, Cho S.

    09/6/2014
    Hepatic triacylglycerol synthesis and secretion: DGAT2 as the link between glycaemia and triglyceridaemia.

    Hepatic triacylglycerol synthesis and secretion: DGAT2 as the link between glycaemia and triglyceridaemia.
    Zammit VA.

    05/4/2013
    describe distinct but synergistic roles of the two DGATs in an integrated pathway of TAG synthesis and secretion, with DGAT2 acting upstream of DGAT1

    Diacylglycerol acyltransferase 2 acts upstream of diacylglycerol acyltransferase 1 and utilizes nascent diglycerides and de novo synthesized fatty acids in HepG2 cells.
    Wurie HR, Buckett L, Zammit VA.

    11/17/2012
    Niacin treatment may reduce liver fat content in Chinese patients with dyslipidemia and the mechanism may involve inhibition of DGAT2.

    Liver fat reduction with niacin is influenced by DGAT-2 polymorphisms in hypertriglyceridemic patients.
    Hu M, Chu WC, Yamashita S, Yeung DK, Shi L, Wang D, Masuda D, Yang Y, Tomlinson B., Free PMC Article

    07/7/2012
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
    DGAT2, an ER-resident transmembrane domain-containing enzyme, is also found in mitochondria-associated membranes, where its N terminus may promote its association with mitochondria.

    The endoplasmic reticulum enzyme DGAT2 is found in mitochondria-associated membranes and has a mitochondrial targeting signal that promotes its association with mitochondria.
    Stone SJ, Levin MC, Zhou P, Han J, Walther TC, Farese RV Jr., Free PMC Article

    01/21/2010
    Review summarizes current knowledge of DGAT1 and DGAT2 enzymes, focusing on new advances since the cloning of their genes, including possible roles in human health and diseases.

    Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis.
    Yen CL, Stone SJ, Koliwad S, Harris C, Farese RV Jr., Free PMC Article

    01/21/2010
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