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Volumn 428, Issue 16, 2016, Pages 3295-3304

The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase

Author keywords

FAS; lipogenesis; liver; O GlcNAcylation; ob ob mice

Indexed keywords

DEUBIQUITINASE; FATTY ACID; FATTY ACID SYNTHASE; GLYCOSIDASE INHIBITOR; N ACETYL BETA GLUCOSAMINIDASE; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINYLTRANSFERASE; THIAMET G; UBIQUITIN SPECIFIC PROTEASE 2A; UNCLASSIFIED DRUG; O-GLCNAC TRANSFERASE;

EID: 84969962012     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2016.04.035     Document Type: Article
Times cited : (46)

References (34)
  • 1
    • 84939621718 scopus 로고    scopus 로고
    • Functional roles of fatty acids and their effects on human health
    • [1] Calder, P.C., Functional roles of fatty acids and their effects on human health. J. Parenter. Enter. Nutr. 39 (2015), 18S–32S.
    • (2015) J. Parenter. Enter. Nutr. , vol.39 , pp. 18S-32S
    • Calder, P.C.1
  • 2
    • 0028085233 scopus 로고
    • Regulation of lipogenic enzyme gene expression by nutrients and hormones
    • [2] Girard, J., Perdereau, D., Foufelle, F., Prip-Buus, C., Ferré, P., Regulation of lipogenic enzyme gene expression by nutrients and hormones. FASEB J. 8 (1994), 36–42.
    • (1994) FASEB J. , vol.8 , pp. 36-42
    • Girard, J.1    Perdereau, D.2    Foufelle, F.3    Prip-Buus, C.4    Ferré, P.5
  • 3
    • 18244382304 scopus 로고    scopus 로고
    • Sources of fatty acids stored in liver and secreted via lipoproteins in patients with nonalcoholic fatty liver disease
    • [3] Donnelly, K.L., Smith, C.I., Schwarzenberg, S.J., Jessurun, J., Boldt, M.D., Parks, E.J., Sources of fatty acids stored in liver and secreted via lipoproteins in patients with nonalcoholic fatty liver disease. J. Clin. Invest. 115 (2005), 1343–1351.
    • (2005) J. Clin. Invest. , vol.115 , pp. 1343-1351
    • Donnelly, K.L.1    Smith, C.I.2    Schwarzenberg, S.J.3    Jessurun, J.4    Boldt, M.D.5    Parks, E.J.6
  • 4
    • 0025855139 scopus 로고
    • Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance
    • [4] Marshall, S., Bacote, V., Traxinger, R.R., Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J. Biol. Chem. 266 (1991), 4706–4712.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 5
    • 77949295164 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine
    • [5] Hanover, J.A., Krause, M.W., Love, D.C., The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine. Biochim. Biophys. Acta. 1800 (2010), 80–95.
    • (2010) Biochim. Biophys. Acta. , vol.1800 , pp. 80-95
    • Hanover, J.A.1    Krause, M.W.2    Love, D.C.3
  • 6
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • [6] Torres, C.R., Hart, G.W., Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259 (1984), 3308–3317.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 7
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • [7] Kreppel, L.K., Blomberg, M.A., Hart, G.W., Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272 (1997), 9308–9315.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 8
    • 58649095123 scopus 로고    scopus 로고
    • Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose
    • [8] Hu, Y., Suarez, J., Fricovsky, E., Wang, H., Scott, B.T., Trauger, S.A., et al. Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. J. Biol. Chem. 284 (2009), 547–555.
    • (2009) J. Biol. Chem. , vol.284 , pp. 547-555
    • Hu, Y.1    Suarez, J.2    Fricovsky, E.3    Wang, H.4    Scott, B.T.5    Trauger, S.A.6
  • 9
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
    • [9] Gao, Y., Wells, L., Comer, F.I., Parker, G.J., Hart, G.W., Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. J. Biol. Chem. 276 (2001), 9838–9845.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 10
    • 77949283280 scopus 로고    scopus 로고
    • Dysregulation of the nutrient/stress sensor O-GlcNAcylation is involved in the etiology of cardiovascular disorders, type-2 diabetes and Alzheimer's disease
    • [10] Lefebvre, T., Dehennaut, V., Guinez, C., Olivier, S., Drougat, L., Mir, A.-M., et al. Dysregulation of the nutrient/stress sensor O-GlcNAcylation is involved in the etiology of cardiovascular disorders, type-2 diabetes and Alzheimer's disease. Biochim. Biophys. Acta. 1800 (2010), 67–79.
    • (2010) Biochim. Biophys. Acta. , vol.1800 , pp. 67-79
    • Lefebvre, T.1    Dehennaut, V.2    Guinez, C.3    Olivier, S.4    Drougat, L.5    Mir, A.-M.6
  • 12
    • 84916878247 scopus 로고    scopus 로고
    • O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat
    • [12] Ruan, H.B., Dietrich, M.O., Liu, Z.W., Zimmer, M.R., Li, M.D., Singh, J.P., et al. O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat. Cell. 159 (2014), 306–317.
    • (2014) Cell. , vol.159 , pp. 306-317
    • Ruan, H.B.1    Dietrich, M.O.2    Liu, Z.W.3    Zimmer, M.R.4    Li, M.D.5    Singh, J.P.6
  • 13
    • 37349081571 scopus 로고    scopus 로고
    • Role of ChREBP in hepatic steatosis and insulin resistance
    • [13] Denechaud, P.-D., Dentin, R., Girard, J., Postic, C., Role of ChREBP in hepatic steatosis and insulin resistance. FEBS Lett. 582 (2008), 68–73.
    • (2008) FEBS Lett. , vol.582 , pp. 68-73
    • Denechaud, P.-D.1    Dentin, R.2    Girard, J.3    Postic, C.4
  • 14
    • 79959473762 scopus 로고    scopus 로고
    • O-GlcNAcylation increases ChREBP protein content and transcriptional activity in the liver
    • [14] Guinez, C., Filhoulaud, G., Rayah-Benhamed, F., Marmier, S., Dubuquoy, C., Dentin, R., et al. O-GlcNAcylation increases ChREBP protein content and transcriptional activity in the liver. Diabetes. 60 (2011), 1399–1413.
    • (2011) Diabetes. , vol.60 , pp. 1399-1413
    • Guinez, C.1    Filhoulaud, G.2    Rayah-Benhamed, F.3    Marmier, S.4    Dubuquoy, C.5    Dentin, R.6
  • 16
    • 0034669025 scopus 로고    scopus 로고
    • Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta
    • [16] Repa, J.J., Liang, G., Ou, J., Bashmakov, Y., Lobaccaro, J.M., Shimomura, I., et al. Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta. Genes Dev. 14 (2000), 2819–2830.
    • (2000) Genes Dev. , vol.14 , pp. 2819-2830
    • Repa, J.J.1    Liang, G.2    Ou, J.3    Bashmakov, Y.4    Lobaccaro, J.M.5    Shimomura, I.6
  • 17
    • 33847006599 scopus 로고    scopus 로고
    • The liver X receptor (LXR) and hepatic lipogenesis. The carbohydrate-response element-binding protein is a target gene of LXR
    • [17] Cha, J.-Y., Repa, J.J., The liver X receptor (LXR) and hepatic lipogenesis. The carbohydrate-response element-binding protein is a target gene of LXR. J. Biol. Chem. 282 (2007), 743–751.
    • (2007) J. Biol. Chem. , vol.282 , pp. 743-751
    • Cha, J.-Y.1    Repa, J.J.2
  • 18
    • 9444242641 scopus 로고    scopus 로고
    • Impact of adenoviral transduction with SREBP1c or AMPK on pancreatic islet gene expression profile: analysis with oligonucleotide microarrays
    • [18] Diraison, F., Motakis, E., Parton, L.E., Nason, G.P., Leclerc, I., Rutter, G.A., Impact of adenoviral transduction with SREBP1c or AMPK on pancreatic islet gene expression profile: analysis with oligonucleotide microarrays. Diabetes. 53 (2004), S84–591.
    • (2004) Diabetes. , vol.53 , pp. S84-591
    • Diraison, F.1    Motakis, E.2    Parton, L.E.3    Nason, G.P.4    Leclerc, I.5    Rutter, G.A.6
  • 19
    • 84927593686 scopus 로고    scopus 로고
    • Liver X receptor regulates hepatic nuclear O-GlcNAc signaling and carbohydrate responsive element-binding protein activity
    • [19] Bindesbøll, C., Fan, Q., Nørgaard, R.C., MacPherson, L., Ruan, H.-B., Wu, J., et al. Liver X receptor regulates hepatic nuclear O-GlcNAc signaling and carbohydrate responsive element-binding protein activity. J. Lipid Res. 56 (2015), 771–785.
    • (2015) J. Lipid Res. , vol.56 , pp. 771-785
    • Bindesbøll, C.1    Fan, Q.2    Nørgaard, R.C.3    MacPherson, L.4    Ruan, H.-B.5    Wu, J.6
  • 21
    • 78651081729 scopus 로고    scopus 로고
    • Effects of farnesoid X receptor on the expression of the fatty acid synthetase and hepatic lipase
    • [21] Shen, L.-L., Liu, H., Peng, J., Gan, L., Lu, L., Zhang, Q., et al. Effects of farnesoid X receptor on the expression of the fatty acid synthetase and hepatic lipase. Mol. Biol. Rep. 38 (2011), 553–559.
    • (2011) Mol. Biol. Rep. , vol.38 , pp. 553-559
    • Shen, L.-L.1    Liu, H.2    Peng, J.3    Gan, L.4    Lu, L.5    Zhang, Q.6
  • 22
    • 84899475842 scopus 로고    scopus 로고
    • Glucose sensing O-GlcNAcylation pathway regulates the nuclear bile acid receptor farnesoid X receptor (FXR)
    • [22] Berrabah, W., Aumercier, P., Gheeraert, C., Dehondt, H., Bouchaert, E., Alexandre, J., et al. Glucose sensing O-GlcNAcylation pathway regulates the nuclear bile acid receptor farnesoid X receptor (FXR). Hepatology. 59 (2014), 2022–2033.
    • (2014) Hepatology. , vol.59 , pp. 2022-2033
    • Berrabah, W.1    Aumercier, P.2    Gheeraert, C.3    Dehondt, H.4    Bouchaert, E.5    Alexandre, J.6
  • 23
    • 84890731711 scopus 로고    scopus 로고
    • Regulation of protein degradation by O-GlcNAcylation: crosstalk with ubiquitination
    • [23] Ruan, H.-B., Nie, Y., Yang, X., Regulation of protein degradation by O-GlcNAcylation: crosstalk with ubiquitination. Mol. Cell. Proteomics. 12 (2013), 3489–3497.
    • (2013) Mol. Cell. Proteomics. , vol.12 , pp. 3489-3497
    • Ruan, H.-B.1    Nie, Y.2    Yang, X.3
  • 24
    • 84905216343 scopus 로고    scopus 로고
    • O-GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41
    • [24] Olivier-Van Stichelen, S., Dehennaut, V., Buzy, A., Zachayus, J.-L., Guinez, C., Mir, A.-M., et al. O-GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41. FASEB J. 28 (2014), 3325–3338.
    • (2014) FASEB J. , vol.28 , pp. 3325-3338
    • Olivier-Van Stichelen, S.1    Dehennaut, V.2    Buzy, A.3    Zachayus, J.-L.4    Guinez, C.5    Mir, A.-M.6
  • 25
    • 84864708480 scopus 로고    scopus 로고
    • O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability
    • [25] Ruan, H.-B., Han, X., Li, M.-D., Singh, J.P., Qian, K., Azarhoush, S., et al. O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability. Cell Metab. 16 (2012), 226–237.
    • (2012) Cell Metab. , vol.16 , pp. 226-237
    • Ruan, H.-B.1    Han, X.2    Li, M.-D.3    Singh, J.P.4    Qian, K.5    Azarhoush, S.6
  • 26
    • 78449288408 scopus 로고    scopus 로고
    • Snail1 is stabilized by O-GlcNAc modification in hyperglycaemic condition
    • [26] Park, S.Y., Kim, H.S., Kim, N.H., Ji, S., Cha, S.Y., Kang, J.G., et al. Snail1 is stabilized by O-GlcNAc modification in hyperglycaemic condition. EMBO J. 29 (2010), 3787–3796.
    • (2010) EMBO J. , vol.29 , pp. 3787-3796
    • Park, S.Y.1    Kim, H.S.2    Kim, N.H.3    Ji, S.4    Cha, S.Y.5    Kang, J.G.6
  • 27
    • 84956634607 scopus 로고    scopus 로고
    • Mixed lineage leukemia 5 (MLL5) protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin specific protease 7 (USP7)
    • e0145023
    • [27] Ding, X., Jiang, W., Zhou, P., Liu, L., Wan, X., Yuan, X., et al. Mixed lineage leukemia 5 (MLL5) protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin specific protease 7 (USP7). PLoS One, 10(12), 2015, e0145023, 10.1371/journal.pone.0145023.
    • (2015) PLoS One , vol.10 , Issue.12
    • Ding, X.1    Jiang, W.2    Zhou, P.3    Liu, L.4    Wan, X.5    Yuan, X.6
  • 28
    • 84926432212 scopus 로고    scopus 로고
    • Effects of puerarin on lipid accumulation and metabolism in high-fat diet-fed mice
    • e0122925
    • [28] Zheng, G., Lin, L., Zhong, S., Zhang, Q., Li, D., Effects of puerarin on lipid accumulation and metabolism in high-fat diet-fed mice. PLoS One, 10(3), 2015, e0122925, 10.1371/journal.pone.0122925.
    • (2015) PLoS One , vol.10 , Issue.3
    • Zheng, G.1    Lin, L.2    Zhong, S.3    Zhang, Q.4    Li, D.5
  • 29
    • 34848880141 scopus 로고    scopus 로고
    • Nicotine-induced activation of AMP-activated protein kinase inhibits fatty acid synthase in 3T3L1 adipocytes a ROLE FOR OXIDANT STRESS
    • [29] An, Z., Wang, H., Song, P., Zhang, M., Geng, X., Zou, M.-H., Nicotine-induced activation of AMP-activated protein kinase inhibits fatty acid synthase in 3T3L1 adipocytes a ROLE FOR OXIDANT STRESS. J. Biol. Chem. 282 (2007), 26,793–26,801.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26793-26801
    • An, Z.1    Wang, H.2    Song, P.3    Zhang, M.4    Geng, X.5    Zou, M.-H.6
  • 30
    • 78149494317 scopus 로고    scopus 로고
    • Fatty acid synthase phosphorylation: a novel therapeutic target in HER2-overexpressing breast cancer cells
    • [30] Jin, Q., Yuan, L.X., Boulbes, D., Baek, J.M., Wang, Y.N., Gomez-Cabello, D., et al. Fatty acid synthase phosphorylation: a novel therapeutic target in HER2-overexpressing breast cancer cells. Breast Cancer Res., 12, 2010, R96.
    • (2010) Breast Cancer Res. , vol.12 , pp. R96
    • Jin, Q.1    Yuan, L.X.2    Boulbes, D.3    Baek, J.M.4    Wang, Y.N.5    Gomez-Cabello, D.6
  • 32
    • 84958160165 scopus 로고    scopus 로고
    • O-GlcNAcylation and the metabolic shift in high-proliferating cells: all the evidence suggests that sugars dictate the flux of lipid biogenesis in tumor processes
    • [32] Baldini, S.F., Lefebvre, T., O-GlcNAcylation and the metabolic shift in high-proliferating cells: all the evidence suggests that sugars dictate the flux of lipid biogenesis in tumor processes. Front. Oncol., 6, 2016, 6.
    • (2016) Front. Oncol. , vol.6 , pp. 6
    • Baldini, S.F.1    Lefebvre, T.2
  • 33
    • 12144286902 scopus 로고    scopus 로고
    • The isopeptidase USP2a regulates the stability of fatty acid synthase in prostate cancer
    • [33] Graner, E., Tang, D., Rossi, S., Baron, A., Migita, T., Weinstein, L.J., et al. The isopeptidase USP2a regulates the stability of fatty acid synthase in prostate cancer. Cancer Cell. 5 (2004), 253–261.
    • (2004) Cancer Cell. , vol.5 , pp. 253-261
    • Graner, E.1    Tang, D.2    Rossi, S.3    Baron, A.4    Migita, T.5    Weinstein, L.J.6
  • 34
    • 33746820622 scopus 로고    scopus 로고
    • The isopeptidase USP2a protects human prostate cancer from apoptosis
    • [34] Priolo, C., Tang, D., Brahamandan, M., Benassi, B., Sicinska, E., Ogino, S., et al. The isopeptidase USP2a protects human prostate cancer from apoptosis. Cancer Res. 66 (2006), 8625–8632.
    • (2006) Cancer Res. , vol.66 , pp. 8625-8632
    • Priolo, C.1    Tang, D.2    Brahamandan, M.3    Benassi, B.4    Sicinska, E.5    Ogino, S.6


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