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    MGAT1 alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase [ Homo sapiens (human) ]

    Gene ID: 4245, updated on 12-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Elucidating the multifaceted role of MGAT1 in hepatocellular carcinoma: integrative single-cell and spatial transcriptomics reveal novel therapeutic insights.

    Elucidating the multifaceted role of MGAT1 in hepatocellular carcinoma: integrative single-cell and spatial transcriptomics reveal novel therapeutic insights.
    Li Y, Chen Y, Wang D, Wu L, Li T, An N, Yang H., Free PMC Article

    08/1/2024
    MicroRNA miR-331-3p suppresses osteosarcoma progression via the Bcl-2/Bax and Wnt/beta-Catenin signaling pathways and the epithelial-mesenchymal transition by targeting N-acetylglucosaminyltransferase I (MGAT1).

    MicroRNA miR-331-3p suppresses osteosarcoma progression via the Bcl-2/Bax and Wnt/β-Catenin signaling pathways and the epithelial-mesenchymal transition by targeting N-acetylglucosaminyltransferase I (MGAT1).
    Bi W, Yang M, Xing P, Huang T., Free PMC Article

    07/9/2022
    Point mutations that inactivate MGAT4D-L, an inhibitor of MGAT1 and complex N-glycan synthesis.

    Point mutations that inactivate MGAT4D-L, an inhibitor of MGAT1 and complex N-glycan synthesis.
    Akintayo A, Mayoral J, Asada M, Tang J, Sundaram S, Stanley P., Free PMC Article

    02/20/2021
    MGAT1 promotes complex N-glycosylation of glucose transporter 1 (Glut1) and increases Glut1 protein levels. In summary, our findings indicate that MGAT1 is highly expressed in glioblastoma and promotes glioma cells at least partly through upregulation of Glut1 protein.

    N-acetylglucosaminyltransferase I promotes glioma cell proliferation and migration through increasing the stability of the glucose transporter GLUT1.
    Li Y, Liu Y, Zhu H, Chen X, Tian M, Wei Y, Gong Y, Jiang J.

    07/25/2020
    MGAT1 activity may play a role in regulating basal adipocyte FFA retention

    Metabolic importance of adipose tissue monoacylglycerol acyltransferase 1 in mice and humans.
    Liss KHH, Lutkewitte AJ, Pietka T, Finck BN, Franczyk M, Yoshino J, Klein S, Hall AM., Free PMC Article

    09/14/2019
    In this study we showed that the activation of Wnt/beta-catenin pathway culminates in the upregulation of MGAT1 enzyme both at transcriptional and post-transcriptional levels. We also showed that overexpression of the beta-catenin gene (CTNNB1) increased the promoter activity of MGAT1.

    MGAT1 is a novel transcriptional target of Wnt/β-catenin signaling pathway.
    Akiva I, Birgül Iyison N., Free PMC Article

    08/11/2018
    The presence of the rs4285184 polymorphism of the MGAT1 gene increased the risk for developing body fat associated with obesity in the Mexican population.

    The rs4285184 polymorphism of the MGAT1 gene as a risk factor for obesity in the Mexican population.
    Tapia-Rivera JC, Baltazar-Rodríguez LM, Cárdenas-Rojas MI, Álvarez A, Bustos-Saldaña R, Delgado-Enciso I, Valdez-Velázquez LL, Guzmán-Esquivel J, Ramírez-Flores M.

    01/13/2018
    MGAT1 is downregulated in peripheral blood mononuclear cells of galactosaemia patients.

    Classical galactosaemia: novel insights in IgG N-glycosylation and N-glycan biosynthesis.
    Maratha A, Stockmann H, Coss KP, Estela Rubio-Gozalbo M, Knerr I, Fitzgibbon M, McVeigh TP, Foley P, Moss C, Colhoun HO, van Erven B, Stephens K, Doran P, Rudd P, Treacy E., Free PMC Article

    07/29/2017
    The authors show here that the luminal domain of GnT1IP-L contains its MGAT1 inhibitory activity.

    GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain.
    Huang HH, Hassinen A, Sundaram S, Spiess AN, Kellokumpu S, Stanley P., Free PMC Article

    06/11/2016
    UDP-galactose (SLC35A2) and UDP-N-acetylglucosamine (SLC35A3) Transporters Form Glycosylation-related Complexes with Mannoside Acetylglucosaminyltransferases (Mgats).

    UDP-galactose (SLC35A2) and UDP-N-acetylglucosamine (SLC35A3) Transporters Form Glycosylation-related Complexes with Mannoside Acetylglucosaminyltransferases (Mgats).
    Maszczak-Seneczko D, Sosicka P, Kaczmarek B, Majkowski M, Luzarowski M, Olczak T, Olczak M., Free PMC Article

    02/27/2016
    The IL2RA and IL7RA variants had univariate association in MS and T1D, whereas the MGAT1 and CTLA-4 variants associated with only MS or T1D, respectively.

    Family studies of type 1 diabetes reveal additive and epistatic effects between MGAT1 and three other polymorphisms.
    Yu Z, Li CF, Mkhikian H, Zhou RW, Newton BL, Demetriou M., Free PMC Article

    02/14/2015
    analysis of suppression of cancer progression by MGAT1 shRNA knockdown

    Suppression of cancer progression by MGAT1 shRNA knockdown.
    Beheshti Zavareh R, Sukhai MA, Hurren R, Gronda M, Wang X, Simpson CD, Maclean N, Zih F, Ketela T, Swallow CJ, Moffat J, Rose DR, Schachter H, Schimmer AD, Dennis JW., Free PMC Article

    02/16/2013
    Genetic variants downstream MGAT1 seem to influence susceptibility to obesity. Moreover, these genetic variants affect the levels of serum unsaturated fatty acids and Delta desaturase indices, variables previously shown to correlate with obesity.

    Genetic variants near the MGAT1 gene are associated with body weight, BMI and fatty acid metabolism among adults and children.
    Jacobsson JA, Rask-Andersen M, Risérus U, Moschonis G, Koumpitski A, Chrousos GP, Lannfelt L, Marcus C, Gyllensten U, Schiöth HB, Fredriksson R., Free PMC Article

    03/3/2012
    Activity of HuGnTI in plants is limited by a combination of reduced protein stability, alternative protein targeting and possibly to some extend to lower enzymatic performance of the catalytic domain in the plant biochemical environment.

    Differential effects of human and plant N-acetylglucosaminyltransferase I (GnTI) in plants.
    Henquet M, Heinhuis B, Borst JW, Eigenhuijsen J, Schreuder M, Bosch D, van der Krol A., Free PMC Article

    12/4/2010
    The analysis enabled us to identify a new candidate gene, MGAT1, associated with weight in women.

    Linkage and genome-wide association analysis of obesity-related phenotypes: association of weight with the MGAT1 gene.
    Johansson A, Marroni F, Hayward C, Franklin CS, Kirichenko AV, Jonasson I, Hicks AA, Vitart V, Isaacs A, Axenovich T, Campbell S, Floyd J, Hastie N, Knott S, Lauc G, Pichler I, Rotim K, Wild SH, Zorkoltseva IV, Wilson JF, Rudan I, Campbell H, Pattaro C, Pramstaller P, Oostra BA, Wright AF, van Duijn CM, Aulchenko YS, Gyllensten U, EUROSPAN Consortium, Johansson A, Marroni F, Hayward C, Franklin CS, Kirichenko AV, Jonasson I, Hicks AA, Vitart V, Isaacs A, Axenovich T, Campbell S, Floyd J, Hastie N, Knott S, Lauc G, Pichler I, Rotim K, Wild SH, Zorkoltseva IV, Wilson JF, Rudan I, Campbell H, Pattaro C, Pramstaller P, Oostra BA, Wright AF, van Duijn CM, Aulchenko YS, Gyllensten U, EUROSPAN Consortium.

    09/13/2010
    Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)

    Linkage and genome-wide association analysis of obesity-related phenotypes: association of weight with the MGAT1 gene.
    Johansson A, Marroni F, Hayward C, Franklin CS, Kirichenko AV, Jonasson I, Hicks AA, Vitart V, Isaacs A, Axenovich T, Campbell S, Floyd J, Hastie N, Knott S, Lauc G, Pichler I, Rotim K, Wild SH, Zorkoltseva IV, Wilson JF, Rudan I, Campbell H, Pattaro C, Pramstaller P, Oostra BA, Wright AF, van Duijn CM, Aulchenko YS, Gyllensten U, EUROSPAN Consortium, Johansson A, Marroni F, Hayward C, Franklin CS, Kirichenko AV, Jonasson I, Hicks AA, Vitart V, Isaacs A, Axenovich T, Campbell S, Floyd J, Hastie N, Knott S, Lauc G, Pichler I, Rotim K, Wild SH, Zorkoltseva IV, Wilson JF, Rudan I, Campbell H, Pattaro C, Pramstaller P, Oostra BA, Wright AF, van Duijn CM, Aulchenko YS, Gyllensten U, EUROSPAN Consortium.

    12/2/2009
    Observational study of gene-disease association. (HuGE Navigator)

    Genetic association studies of methamphetamine use disorders: A systematic review and synthesis.
    Bousman CA, Glatt SJ, Everall IP, Tsuang MT.

    03/25/2009
    Findings indicated that cysteine 121 has a structural role in maintaining active site geometry of hGnT1, rather than a catalytic role, and illustrates for the first time the potential utility of E. coli as an expression system for hGnT1.

    Refolding of human beta-1-2 GlcNAc transferase (GnT1) and the role of its unpaired Cys 121.
    Saribas AS, Johnson K, Liu L, Bezila D, Hakes D.

    01/21/2010
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