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Transcriptional regulation of hepatic lipogenesis
Open accessAbstract
Fatty acid and fat synthesis in the liver is a highly regulated metabolic pathway that is important for very low-density lipoprotein (VLDL) production and thus energy distribution to other tissues. Having common features at their promoter regions, lipogenic genes are coordinately regulated at the transcriptional level. Transcription factors, such as upstream stimulatory factors (USFs), sterol regulatory element-binding protein 1C (SREBP1C), liver X receptors (LXRs) and carbohydrate-responsive element-binding protein (ChREBP) have crucial roles in this process. Recently, insights have been gained into the signalling pathways that regulate these transcription factors. After feeding, high blood glucose and insulin levels activate lipogenic genes through several pathways, including the DNA-dependent protein kinase (DNA-PK), atypical protein kinase C (aPKC) and AKT-mTOR pathways. These pathways control the post-translational modifications of transcription factors and co-regulators, such as phosphorylation, acetylation or ubiquitylation, that affect their function, stability and/or localization. Dysregulation of lipogenesis can contribute to hepatosteatosis, which is associated with obesity and insulin resistance.
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“ChREBP, which is a member of the Mondo family of transcription factors, senses carbohydrates and activates genes involved in glycolysis, DNL, and lipid trafficking [2,34,78].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“DNL is minimal during fasting but increases after a meal as glucose and insulin levels rise, activating insulin signaling via PI3K, AKT, aPKC, mTORC, DNA-dependent protein kinase, and phosphatases [34,83].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“However, it decreased in the presence of severe IR [34,94].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“This result also demonstrates that hepatic steatosis is not necessarily accompanied by IR in DNL in the liver and can be initiated by factors other than insulin signaling [34].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“Thus, insulin activates specific kinases and phosphatases that can modify transcription factors such as upstream stimulatory factor (USF), SREBP1c, ChREBP, and liver X receptor (LXR), or regulate the expression of these transcription factors (Fig. 4) [34,83].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“ChREBP, which is activated by carbohydrate uptake [9,34,78,83].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“In this regard, ChREBP expression in liver biopsies from patients with MASH was observed to be two-fold higher when the histologic steatosis score was greater than 50% compared to those with less than 50%.”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“Supporting this perspective, monosaccharides have been shown to activate ChREBP and other key lipogenic transcription factors—including SREBP1c, LXR, and PPARγ—via insulin-independent mechanisms [34,70,83,86,99].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“Additionally, substrate-driven pathways as insulin-independent mechanisms contribute to elevated DNL and enhanced esterification of FFAs into hepatic TG [34,70,85,86].”
From Hepatic Insulin Resistance and Steatosis in Metabolic Dysfunction-Associated Steatotic Liver Disease: New Insights into Mechanisms and Clinical Implications (2025) · cites this paper as [34]
In the citing paper
“VLDL assembly and secretion are upregulated by (i) the delivery of FA released from insulin-resistant adipocytes, (ii) the increased delivery of remnant TG–FA to the liver due to reduced peripheral lipolysis of chylomicron and VLDL–TG, and (iii) the increased de novo lipogenesis55 (Figure 4).”
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Citations
Cites
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
Energy Metabolism in the Liver
Rui, L. (2014) · Comprehensive physiology · doi:10.1002/cphy.c130024 · Cited by 2,401
Repa, J. J., Liang, G., Ou, J., Bashmakov, Y. K., Lobaccaro, J. A., Shimomura, I., Shan, B., Brown, M. S., Goldstein, J. L., & Mangelsdorf, D. J. (2000) · Genes & Development · doi:10.1101/gad.844900 · Cited by 1,724
An oxysterol signalling pathway mediated by the nuclear receptor LXRα
Janowski, B. A., Willy, P. J., Devi, T. R., Falck, J. R., & Mangelsdorf, D. J. (1996) · Nature · doi:10.1038/383728a0 · Cited by 1,591
Role of LXRs in control of lipogenesis
Schultz, J. R., Tu, H., Luk, A., Repa, J. J., Medina, J. C., Li, L., Schwendner, S., Wang, S., Thoolen, M., Mangelsdorf, D. J., et al. (2000) · Genes & Development · doi:10.1101/gad.850400 · Cited by 1,499
Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427
Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
Wang, Z., Zang, C., Cui, K., Schones, D. E., Barski, A., Peng, W., & Zhao, K. (2009) · Cell · doi:10.1016/j.cell.2009.06.049 · Cited by 1,344
mTOR Complex 1 Regulates Lipin 1 Localization to Control the SREBP Pathway
Peterson, T. R., Sengupta, S., Harris, T. E., Carmack, A. E., Kang, S. A., Balderas, E., Guertin, D. A., Madden, K. L., Carpenter, A. E., Finck, B. N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.034 · Cited by 1,293
Regulation of circadian behaviour and metabolism by REV-ERB-α and REV-ERB-β
Cho, H., Zhao, X., Hatori, M., Yu, R. T., Barish, G. D., Lam, M. T., Chong, L.-W., DiTacchio, L., Atkins, A. R., Glass, C. K., et al. (2012) · Nature · doi:10.1038/nature11048 · Cited by 1,037
Time for food: the intimate interplay between nutrition, metabolism, and the circadian clock
Asher, G., & Sassone-Corsi, P. (2015) · Cell · doi:10.1016/j.cell.2015.03.015 · Cited by 844
A Topoisomerase IIß-Mediated dsDNA Break Required for Regulated Transcription
Ju, B., Lunyak, V. V., Perissi, V., García-Bassets, I., Rose, D. W., Glass, C. K., & Rosenfeld, M. G. (2006) · Science · doi:10.1126/science.1127196 · Cited by 842
Iizuka, K., Bruick, R. K., Liang, G., Horton, J. D., & Uyeda, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401516101 · Cited by 834
Joseph, S. B., Laffitte, B. A., Patel, P. H., Watson, M. A., Matsukuma, K. E., Walczak, R., Collins, J. L., Osborne, T. F., & Tontonoz, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111041200 · Cited by 795
Kim, J. B., Sarraf, P., Wright, M., Yao, K., Mueller, E., Solanes, G., Lowell, B. B., & Spiegelman, B. M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1411 · Cited by 792
Li, S., Brown, M. S., & Goldstein, J. L. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914798107 · Cited by 733
Shimano, H., Horton, J. D., Shimomura, I., Hammer, R. E., Brown, M. S., & Goldstein, J. L. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119248 · Cited by 730
A circadian rhythm orchestrated by histone deacetylase 3 controls hepatic lipid metabolism
Feng, D., Liu, T., Sun, Z., Bugge, A., Mullican, S. E., Alenghat, T., Liu, X. S., & Lazar, M. A. (2011) · Science · doi:10.1126/science.1198125 · Cited by 701
Yecies, J. L., Zhang, H., Menon, S., Liu, S., Yecies, D. W., Lipovsky, A. I., Görgün, C. Z., Kwiatkowski, D. J., Hotamışlıgil, G. S., Lee, C., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.06.002 · Cited by 685
Liang, G., Yang, J., Horton, J. D., Hammer, R. E., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111421200 · Cited by 669
A novel ChREBP isoform in adipose tissue regulates systemic glucose metabolism
Herman, M. A., Peroni, O. D., Villoria, J., Schön, M. R., Abumrad, N. A., Blüher, M., Klein, S., & Kahn, B. B. (2012) · Nature · doi:10.1038/nature10986 · Cited by 632
Tontonoz, P., Kim, J. B., Graves, R. A., & Spiegelman, B. M. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.4753-4759.1993 · Cited by 599
Hepatic mTORC2 Activates Glycolysis and Lipogenesis through Akt, Glucokinase, and SREBP1c
Hagiwara, A., Cornu, M., Cybulski, N., Polak, P., Betz, C., Trapani, F., Terracciano, L., Heim, M. H., Rüegg, M. A., & Hall, M. N. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.03.015 · Cited by 585
Chen, G., Liang, G., Ou, J., Goldstein, J. L., & Brown, M. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404297101 · Cited by 570
SIRT1 Deacetylates and Inhibits SREBP-1C Activity in Regulation of Hepatic Lipid Metabolism*
Ponugoti, B., Kim, D.-H., Xiao, Z., Smith, Z., Miao, J., Zang, M., Wu, S.-Y., Chiang, C., Veenstra, T. D., & Kemper, J. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.122978 · Cited by 553
Viollet, B., Foretz, M., Guigas, B., Horman, S., Dentin, R., Bertrand, L., Hue, L., & Andréelli, F. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108506 · Cited by 543
The nuclear receptor LXR is a glucose sensor
Mitro, N., Mak, P. A., Vargas, L., Godio, C., Hampton, E. N., Molteni, V., Kreusch, A., & Sáez, E. (2006) · Nature · doi:10.1038/nature05449 · Cited by 541
Yoshikawa, T., Shimano, H., Amemiya-Kudo, M., Yahagi, N., Hasty, A. H., Matsuzaka, T., Okazaki, H., Tamura, Y., Iizuka, Y., Ohashi, K., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.9.2991-3000.2001 · Cited by 526
FoxO1 Regulates Multiple Metabolic Pathways in the Liver
Zhang, W., Patil, S., Chauhan, B., Guo, S., Powell, D. R., Le, J., Klotsas, A., Matika, R. W., Xiao, X., Franks, R. R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600272200 · Cited by 522
Rev-erbα and Rev-erbβ coordinately protect the circadian clock and normal metabolic functionPreprint
Bugge, A. K., Feng, D., Everett, L. J., Briggs, E. R., Mullican, S. E., Wang, F., Jager, J., & Lazar, M. A. (2012) · Genes & Development · doi:10.1101/gad.186858.112 · Cited by 514
The Liver X Receptor (LXR) and Hepatic Lipogenesis
Cha, J.-Y., & Repa, J. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605023200 · Cited by 502
Giguère, V., Tini, M., Flock, G. B., Ong, E. S., Evans, R. M., & Otulakowski, G. (1994) · Genes & Development · doi:10.1101/gad.8.5.538 · Cited by 496
Liver-Specific Inhibition of ChREBP Improves Hepatic Steatosis and Insulin Resistance in ob/ob Mice
Dentin, R., Benhamed, F., Hainault, I., Fauveau, V., Foufelle, F., Dyck, J. R. B., Girard, J. R., & Postic, C. (2006) · Diabetes · doi:10.2337/db06-0200 · Cited by 461
Stiles, B., Wang, Y., Stahl, A., Bassilian, S., Lee, W. P., Kim, Y.-J., Sherwin, R., Devaskar, S., Lesche, R., Magnuson, M. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308617100 · Cited by 436
Self-citationMechanism for Fatty Acid “Sparing” Effect on Glucose-induced Transcription
Kawaguchi, T., Osatomi, K., Yamashita, H., Kabashima, T., & Uyeda, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107895200 · Cited by 424
Benhamed, F., Denechaud, P.-D., Lemoine, M., Robichon, C., Moldes, M., Bertrand-Michel, J., Ratziu, V., Serfaty, L., Housset, C., Capeau, J., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci41636 · Cited by 408
Kabashima, T., Kawaguchi, T., Wadzinski, B. E., & Uyeda, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730817100 · Cited by 401
Shimano, H., Shimomura, I., Hammer, R. E., Herz, J., Goldstein, J. L., Brown, M. S., & Horton, J. D. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119746 · Cited by 395
Jiang, T., Wang, Z., Proctor, G., Moskowitz, S., Liebman, S. E., Rogers, T. E., Lucia, M. S., Li, J., & Levi, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500801200 · Cited by 389
ChREBP•Mlx Is the Principal Mediator of Glucose-induced Gene Expression in the Liver
Ma, L., Robinson, L. N., & Towle, H. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601576200 · Cited by 387
Kawaguchi, T., Takenoshita, M., Kabashima, T., & Uyeda, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231370798 · Cited by 373
A Central Role for mTOR in Lipid Homeostasis
Lamming, D. W., & Sabatini, D. M. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.08.002 · Cited by 370
MECHANISMS BY WHICH CARBOHYDRATES REGULATE EXPRESSION OF GENES FOR GLYCOLYTIC AND LIPOGENIC ENZYMES
Girard, J. R., Ferré, P., & Foufelle, F. (1997) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.17.1.325 · Cited by 367
Walker, A. K., Yang, F., Jiang, K., Ji, J.-Y., Watts, J. L., Purushotham, A., Boss, O., Hirsch, M. L., Ribich, S., Smith, J. J., et al. (2010) · Genes & Development · doi:10.1101/gad.1901210 · Cited by 357
Smith, E. M., FINN, S. G., Tee, A. R., Browne, G. J., & Proud, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414499200 · Cited by 354
Familial combined hyperlipidemia is associated with upstream transcription factor 1 (USF1)
Pajukanta, P., Lilja, H. E., Sinsheimer, J. S., Cantor, R. M., Lusis, A. J., Gentile, M., Duan, X. J., Soro‐Paavonen, A., Naukkarinen, J., Saarela, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1320 · Cited by 347
Enzymatic Reduction of Oxysterols Impairs LXR Signaling in Cultured Cells and the Livers of Mice
Chen, W., Chen, G., Head, D. L., Mangelsdorf, D. J., & Russell, D. W. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.11.012 · Cited by 325
Kim, J. B., Spotts, G. D., Halvorsen, Y. C., Shih, H., Ellenberger, T., Towle, H. C., & Spiegelman, B. M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.5.2582 · Cited by 320
Bricambert, J., Miranda, J., Benhamed, F., Girard, J. R., Postic, C., & Dentin, R. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41624 · Cited by 318
De novo lipogenesis in human fat and liver is linked to ChREBP-β and metabolic health
Eissing, L., Scherer, T., Tödter, K., Knippschild, U., Greve, J. W. M., Buurman, W. A., Pinnschmidt, H. O., Rensen, S. S., Wolf, A. M., Bartelt, A., et al. (2013) · Nature Communications · doi:10.1038/ncomms2537 · Cited by 317
LXRs regulate the balance between fat storage and oxidation
Kalaany, N. Y., Gauthier, K. C., Zavacki, A. M., Mammen, P. P. A., Kitazume, T., Peterson, J. A., Horton, J. D., Garry, D. J., Bianco, A. C., & Mangelsdorf, D. J. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.03.001 · Cited by 309
Insulin stimulation of SREBP-1c processing in transgenic rat hepatocytes requires p70 S6-kinase
Owen, J. L., Zhang, Y., Bae, S., Farooqi, M. S., Liang, G., Hammer, R. E., Goldstein, J. L., & Brown, M. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213343109 · Cited by 305
Liver-specific mRNA for Insig-2 down-regulated by insulin: Implications for fatty acid synthesis
Yabe, D., Komuro, R., Liang, G., Goldstein, J. L., & Brown, M. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0130116100 · Cited by 296
Connecting mTORC1 signaling to SREBP-1 activation
Bakan, I., & Laplante, M. (2012) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e328352dd03 · Cited by 291
Insulin signalling mechanisms for triacylglycerol storage
Czech, M., Tencerová, M., Pedersen, D. J., & Aouadi, M. (2013) · Diabetologia · doi:10.1007/s00125-013-2869-1 · Cited by 289
Taniguchi, C. M., Kondo, T., Sajan, M. P., Luo, J., Bronson, R. T., Asano, T., Farese, R. V., Cantley, L. C., & Kahn, C. R. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.005 · Cited by 288
Yin, L., & Lazar, M. A. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0057 · Cited by 283
Sul, H. S., & Wang, D. (1998) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.18.1.331 · Cited by 280
Self-citationLópez, J. M., Bennett, M. K., Sanchez, H. B., Rosenfeld, J. M., & Osborne, T. F. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1049 · Cited by 262
A Role of DNA-PK for the Metabolic Gene Regulation in Response to Insulin
Wong, R. H.-F., Chang, I., Hudak, C. S. S., Hyun, S., Kwan, H. Y., & Sul, H. S. (2009) · Cell · doi:10.1016/j.cell.2008.12.040 · Cited by 258
Self-citationHormonal Regulation of Mouse Fatty Acid Synthase Gene Transcription in Liver
Paulauskis, J. D., & Sul, H. S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31298-x · Cited by 255
Self-citationThe nuclear receptor REV-ERBα is required for the daily balance of carbohydrate and lipid metabolism
Delezie, J., Dumont, S., Dardente, H., Oudart, H., Gréchez‐Cassiau, A., Klosen, P., Teboul, M., Delaunay, F., Pévet, P., & Challet, E. (2012) · The FASEB Journal · doi:10.1096/fj.12-208751 · Cited by 252
Sun, Z., Feng, D., Fang, B., Mullican, S. E., You, S.-H., Lim, H., Everett, L. J., Nabel, C. S., Li, Y., Selvakumaran, V., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.022 · Cited by 251
Wagner, B. L., Valledor, A. F., Shao, G. Q., Daige, C. L., Bischoff, E. D., Petrowski, M. L., Jepsen, K., Baek, S. H., Heyman, R. A., Rosenfeld, M. G., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5780-5789.2003 · Cited by 245
Stoeckman, A. K., Ma, L., & Towle, H. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311301200 · Cited by 237
A diurnal serum lipid integrates hepatic lipogenesis and peripheral fatty acid use
Liu, S., Brown, J. D., Stanya, K. J., Homan, E. A., Leidl, M., Inouye, K., Bhargava, P., Gangl, M. R., Dai, L., Hatano, B., et al. (2013) · Nature · doi:10.1038/nature12710 · Cited by 237
O -GlcNAcylation Increases ChREBP Protein Content and Transcriptional Activity in the Liver
Guinez, C., Filhoulaud, G., Benhamed, F., Marmier, S., Dubuquoy, C., Dentin, R., Moldes, M., Burnol, A., Yang, X., Lefebvre, T., et al. (2011) · Diabetes · doi:10.2337/db10-0452 · Cited by 228
Promoter Analysis of the Mouse Sterol Regulatory Element-binding Protein-1c Gene
Amemiya-Kudo, M., Shimano, H., Yoshikawa, T., Yahagi, N., Hasty, A. H., Okazaki, H., Tamura, Y., Shionoiri, F., Iizuka, Y., Ohashi, K., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005353200 · Cited by 226
ChREBP, but not LXRs, is required for the induction of glucose-regulated genes in mouse liver
Denechaud, P., Bossard, P., Lobaccaro, J. A., Millatt, L. J., Staels, B., Girard, J. R., & Postic, C. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34314 · Cited by 223
Liver X Receptors as Insulin-mediating Factors in Fatty Acid and Cholesterol Biosynthesis
Tobin, K. A. R., Ulven, S. M., Schuster, G. U., Steineger, H. H., Andresen, S. M., Gustafsson, J.-Α., & Nebb, H. I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109771200 · Cited by 212
Novel insights into ChREBP regulation and function
Filhoulaud, G., Guilmeau, S., Dentin, R., Girard, J. R., & Postic, C. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.01.003 · Cited by 211
Direct Role of ChREBP·Mlx in Regulating Hepatic Glucose-responsive Genes
Ma, L., Tsatsos, N. G., & Towle, H. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413063200 · Cited by 195
Haeusler, R. A., Hartil, K., Vaitheesvaran, B., Arrieta‐Cruz, I., Knight, C. M., Cook, J. R., Kammoun, H. L., Febbraio, M. A., Juárez, R. G., Kurland, I. J., et al. (2014) · Nature Communications · doi:10.1038/ncomms6190 · Cited by 192
Cretenet, G., Clech, M. L., & Gachon, F. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2009.11.002 · Cited by 187
Circadian metabolism in the light of evolution
Gerhart-Hines, Z., & Lazar, M. A. (2015) · Endocrine Reviews · doi:10.1210/er.2015-1007 · Cited by 178
Dentin, R., Tomás‐Cobos, L., Foufelle, F., Leopold, J. A., Girard, J. R., Postic, C., & Ferré, P. (2011) · Journal of Hepatology · doi:10.1016/j.jhep.2011.07.019 · Cited by 177
Glucose-Dependent Transcriptional Regulation by an Evolutionarily Conserved Glucose-Sensing Module
Li, M. V., Chang, B. H.-J., Imamura, M., Poungvarin, N., & Chan, L. (2006) · Diabetes · doi:10.2337/db05-0822 · Cited by 177
Matsumoto, M., Ogawa, W., Akimoto, K., Inoue, H., Miyake, K., Furukawa, K., Hayashi, Y., Iguchi, H., Matsuki, Y., Hiramatsu, R., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18816 · Cited by 176
Li, S., Liu, C., Li, N., Hao, T., Han, T., HILL, D. E., Vidal, M., & Lin, J. D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.013 · Cited by 170
Insulin signaling in fatty acid and fat synthesis: a transcriptional perspective
Wong, R. H.-F., & Sul, H. S. (2010) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2010.08.004 · Cited by 164
Self-citationYuan, M., Pino, E. C., Wu, L., Kacergis, M. C., & Soukas, A. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.386854 · Cited by 163
Identification of an insulin response element in the fatty acid synthase promoter.
Moustaïd, N., Beyer, R., & Sul, H. S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37507-5 · Cited by 158
Self-citationRoth, G., Kotzka, J., Kremer, L., Lehr, S., Lohaus, C., Meyer, H. E., Krone, W., & Müller‐Wieland, D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005425200 · Cited by 157
Latasa, M.-J., Moon, Y. S., Kim, K., & Sul, H. S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.180306597 · Cited by 157
Self-citationMagaña, M., Koo, S., Towle, H. C., & Osborne, T. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4726 · Cited by 155
Wang, D., & Sul, H. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26367 · Cited by 154
Self-citationMatsumoto, M., Ogawa, W., Akimoto, K., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318816 · Cited by 152
New Facets in the Regulation of Gene Expression by ADP-Ribosylation and Poly(ADP-ribose) Polymerases
Ryu, K. W., Kim, D.-S., & Kraus, W. L. (2015) · Chemical Reviews · doi:10.1021/cr5004248 · Cited by 151
Ligand-Dependent Enhancer Activation Regulated by Topoisomerase-I Activity
Puc, J., Koźbiał, P., Li, W., Tan, Y., Liu, Z., Suter, T., Ohgi, K. A., Zhang, J., Aggarwal, A. K., & Rosenfeld, M. G. (2015) · Cell · doi:10.1016/j.cell.2014.12.023 · Cited by 149
Beaven, S. W., Matveyenko, A. V., Wroblewski, K., Chao, L. C., Wilpitz, D. C., Hsu, T. W., Lentz, J., Drew, B. G., Hevener, A. L., & Tontonoz, P. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.021 · Cited by 145
Liu, Z., Thompson, K. S., & Towle, H. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31457-1 · Cited by 142
Wang, D., & Sul, H. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25420 · Cited by 140
Self-citationYellaturu, C. R., Deng, X., Cagen, L. M., Wilcox, H. G., Mansbach, C. M., Siddiqi, S. A., Park, E. A., Raghow, R., & Elam, M. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805746200 · Cited by 138
Casado, M., Vallet, V. S., Kahn, A., & Vaulont, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2009 · Cited by 137
Yamamoto, T., Shimano, H., Inoue, N., Nakagawa, Y., Matsuzaka, T., Takahashi, A., Yahagi, N., Sone, H., Suzuki, H., Toyoshima, H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611911200 · Cited by 132
Vallet, V. S., Casado, M., Henrion‐Caude, A., Bucchini, D., Raymondjean, M., Kahn, A., & Vaulont, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20175 · Cited by 131
Hwahng, S. H., Ki, S. H., Bae, E. J., Kim, H. E., & Kim, S. G. (2009) · Hepatology · doi:10.1002/hep.22887 · Cited by 129
Self-citationSer1928 Is a Common Site for Cav1.2 Phosphorylation by Protein Kinase C Isoforms
Yang, L., Liu, G., Zakharov, S. I., Morrow, J., Rybin, V. O., Steinberg, S. F., & Marx, S. O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410509200 · Cited by 122
Regulatory Role of Glycogen Synthase Kinase 3 for Transcriptional Activity of ADD1/SREBP1c
Kim, K. H., Song, M. J., Yoo, E. J., Choe, S. S., Park, S. D., & Kim, J. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405522200 · Cited by 122
Wang, D., & Sul, H. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.48.28716 · Cited by 118
Self-citationTranscriptional Coregulators: Fine-Tuning Metabolism
Mouchiroud, L., Eichner, L. J., Shaw, R. J., & Auwerx, J. H. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.027 · Cited by 116
Arden, C., Tudhope, S. J., Petrie, J. L., Al‐Oanzi, Z. H., Cullen, K. S., Lange, A. J., Towle, H. C., & Agius, L. (2012) · Biochemical Journal · doi:10.1042/bj20111280 · Cited by 116
Liver Clock Protein BMAL1 Promotes de Novo Lipogenesis through Insulin-mTORC2-AKT Signaling
Zhang, D., Tong, X., Arthurs, B., Guha, A., Rui, L., Kamath, A., Inoki, K., & Yin, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.567628 · Cited by 115
Functional Characterization of the L-Type Pyruvate Kinase Gene Glucose Response Complex
Guerra, M. J. D., Bergot, M.-O., Martinez, A., Cuif, M., Kahn, A., & Raymondjean, M. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7725 · Cited by 113
Latasa, M.-J., Griffin, M. J., Moon, Y. S., Kang, C., & Sul, H. S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5896-5907.2003 · Cited by 110
Self-citationNuclear Receptor Liver X Receptor Is O-GlcNAc-modified in Response to Glucose
Anthonisen, E. H., Berven, L. L., Holm, S., Nygård, M., Nebb, H. I., & Grønning-Wang, L. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082685 · Cited by 109
Regulation of Nuclear Import/Export of Carbohydrate Response Element-binding Protein (ChREBP)
Sakiyama, H., Wynn, R., Lee, W.-R., Fukasawa, M., Mizuguchi, H., Gardner, K. H., Repa, J. J., & Uyeda, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804308200 · Cited by 106
Glucose-dependent Liver Gene Expression in Upstream Stimulatory Factor 2 −/− Mice
Vallet, V. S., Henrion‐Caude, A., Bucchini, D., Casado, M., Raymondjean, M., Kahn, A., & Vaulont, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.21944 · Cited by 105
Lee, S., Lee, J., Lee, S.-K., & Lee, J. W. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0012 · Cited by 102
Shin, D. H., Paulauskis, J. D., Moustaïd, N., & Sul, H. S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54359-3 · Cited by 97
Self-citationPathway-selective Insulin Resistance and Metabolic Disease: The Importance of Nutrient Flux
Otero, Y. F., Stafford, J. M., & McGuinness, O. P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.576355 · Cited by 97
Kang, H. S., Okamoto, K., Takeda, Y., Beak, J. Y., Gerrish, K., Bortner, C. D., DeGraff, L. M., Wada, T., Xie, W., & Jetten, A. M. (2011) · Physiological Genomics · doi:10.1152/physiolgenomics.00206.2010 · Cited by 95
Sterol regulatory element-binding protein 1 is negatively modulated by PKA phosphorylation
Lu, M. M., & Shyy, J. Y.-J. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00374.2005 · Cited by 89
Athanikar, J. N., Sanchez, H. B., & Osborne, T. F. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5193 · Cited by 88
Wang, Y., Wong, R. H.-F., Tang, T., Hudak, C. S. S., Yang, D., Duncan, R. E., & Sul, H. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.10.028 · Cited by 80
Self-citationHormonal and Nutritional Control of the Fatty Acid Synthase Promoter in Transgenic Mice
Soncini, M., Yet, S., Moon, Y. K., Chun, J.-Y., & Sul, H. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30339 · Cited by 79
Self-citationGriffin, M. J., Wong, R. H.-F., Pandya, N., & Sul, H. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610566200 · Cited by 70
Self-citationBindesbøll, C., Fan, Q., Nørgaard, R. C., MacPherson, L., Ruan, H., Wu, J., Pedersen, T. Å., Steffensen, K. R., Yang, X., Matthews, J. B., et al. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m049130 · Cited by 68
PIASy-Mediated Sumoylation of SREBP1c Regulates Hepatic Lipid Metabolism upon Fasting Signaling
Lee, G. Y., Jang, H., Lee, J. H., Huh, J. Y., Choi, S., Chung, J., & Kim, J. B. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01166-13 · Cited by 66
Kemper, J. K., Choi, S.-E., & Kim, D.-H. (2013) · Vitamins and hormones · doi:10.1016/b978-0-12-407766-9.00016-x · Cited by 65
The role of O-linked GlcNAc modification on the glucose response of ChREBP
Sakiyama, H., Fujiwara, N., Noguchi, T., Eguchi, H., Yoshihara, D., Uyeda, K., & Suzuki, K. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.10.113 · Cited by 61
Bartok, O., Teesalu, M., Ashwal-Fluss, R., Pandey, V., Hanan, M., Rovenko, B. M., Poukkula, M., Havula, E., Moussaieff, A., Vodala, S., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201591385 · Cited by 60
Chanda, D., Li, T., Song, K. H., Kim, Y., Sim, J., Lee, C. H., Chiang, J. Y. L., & Choi, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022244 · Cited by 59
Deng, X., Yellaturu, C. R., Cagen, L. M., Wilcox, H. G., Park, E. A., Raghow, R., & Elam, M. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702228200 · Cited by 58
Characterization of the Murine Mitochondrial Glycerol-3-phosphate Acyltransferase Promoter
Jerkins, A. A., Liu, W. R., Lee, S.-J., & Sul, H. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1416 · Cited by 52
Self-citationER Stress and Lipogenesis: A Slippery Slope toward Hepatic Steatosis
Basseri, S., & Austin, R. C. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.11.013 · Cited by 52
Kotzka, J., Knebel, B., Haas, J., Kremer, L., Jacob, S., Hartwig, S., Nitzgen, U., & Müller‐Wieland, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032609 · Cited by 50
Li, M. V., Chen, W., Poungvarin, N., Imamura, M., & Chan, L. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0560 · Cited by 47
Regulation of Lipogenic Gene Expression by Lysine-specific Histone Demethylase-1 (LSD1)
Abdulla, A., Zhang, Y., Hsu, F.-N., Xiaoli, A. M., Zhao, X., Yang, E. S. T., Ji, J., & Yang, F. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.573659 · Cited by 40
Moon, Y. S., Latasa, M.-J., Kim, K., Wang, D., & Sul, H. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10121 · Cited by 39
Self-citationGe, Q., Huang, N. N., Wynn, R., Li, Y., Du, X., Miller, B., Zhang, H., & Uyeda, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.418855 · Cited by 38
Feldmann, R., Fischer, C., Kodelja, V., Behrens, S., Haas, S. A., Vingron, M., Timmermann, B., Geikowski, A., & Sauer, S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt034 · Cited by 37
Gene Expression Needs a Break to Unwind Before Carrying On
Haince, J.-F., Rouleau, M., & Poirier, G. G. (2006) · Science · doi:10.1126/science.1129808 · Cited by 30
Functional Characterization of the L-Type Pyruvate Kinase Gene Glucose Response Complex
Guerra, M.-J. M. D., Bergot, M.-O., Martinez, A., et al. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7725-7733.1993 · Cited by 28
Zhang, C., Shin, D.-J., & Osborne, T. F. (2005) · Biochemical Journal · doi:10.1042/bj20041514 · Cited by 27
DNA-PK: Relaying the insulin signal to USF in lipogenesis
Wong, R. H. F., & Sul, H. S. (2009) · Cell Cycle · doi:10.4161/cc.8.13.8941 · Cited by 20
Self-citationWnt asymmetry and the terminal division of neuronal progenitors
Bertrand, V., & Hobert, O. (2009) · Cell Cycle · doi:10.4161/cc.8.13.9024 · Cited by 12
A METHOD OF SEPARATING THE ANTERIOR PITUITARY-LIKE HORMONE FROM THE URINE OF PREGNANT WOMEN
Elden, C. A. (1933) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)75905-x · Cited by 5
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Metadata
- Authors
- Wang, Y., Viscarra, J., Kim, S.-J., & Sul, H. S.
- Affiliations
- University of California, Berkeley (US)
- Corresponding author
- Sul, Hei Sook
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2015-10-22
- Volume
- 16
- Issue
- 11
- Pages
- 678-689
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC4884795
- OpenAlex
- W2174107467
- Cited by
- 646
- References
- 135
- Citations by year
- 2026: 24 · 2025: 52 · 2024: 60 · 2023: 71 · 2022: 85 · 2021: 74 · 2020: 84 · 2019: 62 · 2018: 67 · 2017: 49 · 2016: 17 · 2015: 1
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Update notices
- erratum (2015-12-16)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK105671, F32DK105671, R01DK081098, DK081098)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Keywords
- hepatic lipogenesis, transcriptional regulation, upstream stimulatory factor, SREBP-1c, liver X receptor, ChREBP, DNA-dependent protein kinase, atypical protein kinase C, Akt/mTOR signaling, VLDL production, hepatic steatosis, insulin resistance, obesity
- MeSH terms
- Liver X Receptors, Animals, Fatty Acids, Gene Expression Regulation, Lipoproteins, VLDL, Liver, Nuclear Proteins, Protein Kinase C, Protein Processing, Post-Translational, Transcription Factors, Transcription, Genetic, Signal Transduction, Lipogenesis, Proto-Oncogene Proteins c-akt, Mice, Upstream Stimulatory Factors, DNA-Activated Protein Kinase, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Sterol Regulatory Element Binding Protein 1, Orphan Nuclear Receptors, TOR Serine-Threonine Kinases
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