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Acetyl-CoA metabolism in cancer
Open accessAbstract
Few metabolites can claim a more central and versatile role in cell metabolism than acetyl coenzyme A (acetyl-CoA). Acetyl-CoA is produced during nutrient catabolism to fuel the tricarboxylic acid cycle and is the essential building block for fatty acid and isoprenoid biosynthesis. It also functions as a signalling metabolite as the substrate for lysine acetylation reactions, enabling the modulation of protein functions in response to acetyl-CoA availability. Recent years have seen exciting advances in our understanding of acetyl-CoA metabolism in normal physiology and in cancer, buoyed by new mouse models, in vivo stable-isotope tracing approaches and improved methods for measuring acetyl-CoA, including in specific subcellular compartments. Efforts to target acetyl-CoA metabolic enzymes are also advancing, with one therapeutic agent targeting acetyl-CoA synthesis receiving approval from the US Food and Drug Administration. In this Review, we give an overview of the regulation and cancer relevance of major metabolic pathways in which acetyl-CoA participates. We further discuss recent advances in understanding acetyl-CoA metabolism in normal tissues and tumours and the potential for targeting these pathways therapeutically. We conclude with a commentary on emerging nodes of acetyl-CoA metabolism that may impact cancer biology. Acetyl coenzyme A (acetyl-CoA) is a key metabolite in carbohydrate and lipid metabolism and plays a role in signalling through protein acetylation, and the dysregulation of these pathways is a hallmark of various cancers. In this Review, Guertin and Wellen give an overview of acetyl-CoA metabolism in health and in cancer and discuss emerging therapeutic strategies for targeting metabolic pathways involving acetyl-CoA.
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“acetylation relies on acetyl-CoA (Box 1, Figure I); a key node in various metabolic pathways which are commonly dysregulated in cancer [1–3].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [1]
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“Protein acetylation is intrinsically linked to metabolism due to its use of key metabolic intermediate acetyl-CoA [1,52].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [1]
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GEPIA: a web server for cancer and normal gene expression profiling and interactive analyses
Tang, Z., Li, C., Kang, B., Gao, G., Li, C., & Zhang, Z. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx247 · Cited by 9,849
Ferroptosis: mechanisms, biology and role in disease
Jiang, X., Stockwell, B. R., & Conrad, M. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00324-8 · Cited by 7,973
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695
The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis
Bersuker, K., Hendricks, J. M., Li, Z., Magtanong, L., Ford, B., Tang, P. H., Roberts, M. A., Tong, B., Maimone, T. J., Zoncu, R., et al. (2019) · Nature · doi:10.1038/s41586-019-1705-2 · Cited by 3,703
ATP-citrate lyase links cellular metabolism to histone acetylation
Wellen, K. E., Hatzivassiliou, G., Sachdeva, U. M., Bui, T. V., Cross, J. R., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1164097 · Cited by 2,298
Self-citationTargeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252
Posttranscriptional Control of T Cell Effector Function by Aerobic Glycolysis
Chang, C.-H., Curtis, J. D., Maggi, L. B., Faubert, B., Villarino, A. V., O’Sullivan, D., Huang, S. C.-C., van der Windt, G. J. W., Blagih, J., Qiu, J., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.016 · Cited by 2,204
Cellular Fatty Acid Metabolism and Cancer
Currie, E., Schulze, A., Zechner, R., Walther, T. C., & Farese, R. V. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.05.017 · Cited by 2,123
DHODH-mediated ferroptosis defence is a targetable vulnerability in cancer
Mao, C., Liu, X., Zhang, Y., Lei, G., Yan, Y., Lee, H., Koppula, P., Wu, S., Zhuang, L., Fang, B., et al. (2021) · Nature · doi:10.1038/s41586-021-03539-7 · Cited by 2,028
Activation of a metabolic gene regulatory network downstream of mTOR complex 1
Düvel, K., Yecies, J. L., Menon, S., Raman, P., Lipovsky, A. I., Souza, A. L., Triantafellow, E., Ma, Q., Gorski, R., Cleaver, S., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.022 · Cited by 2,020
Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia
Metallo, C. M., Gameiro, P. A., Bell, E. L., Mattaini, K. R., Yang, J., Hiller, K., Jewell, C. M., Johnson, Z. R., Irvine, D. J., Guarente, L., et al. (2012) · Nature · doi:10.1038/nature10602 · Cited by 1,791
The multifaceted roles of fatty acid synthesis in cancer
Röhrig, F., & Schulze, A. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.89 · Cited by 1,651
SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth
Porstmann, T., Santos, C. R., Griffiths, B., Cully, M., Wu, M., Leevers, S., Griffiths, J. R., Chung, Y.-L., & Schulze, A. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.007 · Cited by 1,413
Autophagy-Dependent Anticancer Immune Responses Induced by Chemotherapeutic Agents in Mice
Michaud, M., Martins, I., Sukkurwala, A. Q., Adjemian, S., Ma, Y., Pellegatti, P., Shen, S., Kepp, O., Scoazec, M., Mignot, G., et al. (2011) · Science · doi:10.1126/science.1208347 · Cited by 1,377
Reductive carboxylation supports growth in tumour cells with defective mitochondria
Mullen, A. R., Wheaton, W. W., Jin, E. S., Chen, P.-H., Sullivan, L. B., Cheng, T., Yang, Y., Linehan, W. M., Chandel, N. S., & DeBerardinis, R. J. (2012) · Nature · doi:10.1038/nature10642 · Cited by 1,328
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324
Autophagy promotes immune evasion of pancreatic cancer by degrading MHC-I
Yamamoto, K., Venida, A., Yano, J., Biancur, D. E., Kakiuchi, M., Gupta, S., Sohn, A. S. W., Mukhopadhyay, S., Lin, E. Y., Parker, S. J., et al. (2020) · Nature · doi:10.1038/s41586-020-2229-5 · Cited by 1,240
Energy-stress-mediated AMPK activation inhibits ferroptosis
Lee, H., Zandkarimi, F., Zhang, Y., Meena, J. K., Kim, J., Zhuang, L., Tyagi, S., Ma, L., Westbrook, T. F., Steinberg, G. R., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0461-8 · Cited by 1,157
Adipose-tissue plasticity in health and disease
Sakers, A. P., Siqueira, M. K. D., Seale, P., & Villanueva, C. J. (2022) · Cell · doi:10.1016/j.cell.2021.12.016 · Cited by 1,124
ATP citrate lyase inhibition can suppress tumor cell growth
Hatzivassiliou, G., Zhao, F., Bauer, D. E., Andreadis, C., Shaw, A. N., Dhanak, D., Hingorani, S. R., Tuveson, D. A., & Thompson, C. B. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.09.008 · Cited by 1,086
Lambert, J. E., Ramos–Roman, M. A., Browning, J. D., & Parks, E. J. (2014) · Gastroenterology · doi:10.1053/j.gastro.2013.11.049 · Cited by 1,069
Cell-programmed nutrient partitioning in the tumour microenvironment
Reinfeld, B. I., Madden, M. Z., Wolf, M. M., Chytil, A. M., Bader, J. E., Patterson, A. R., Sugiura, A., Cohen, A. S., Ali, A., Do, B. T., et al. (2021) · Nature · doi:10.1038/s41586-021-03442-1 · Cited by 1,062
Fasting, Circadian Rhythms, and Time-Restricted Feeding in Healthy Lifespan
Longo, V. D., & Panda, S. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.001 · Cited by 1,013
Wise, D. R., Ward, P. S., Shay, J. E. S., Cross, J. R., Gruber, J. J., Sachdeva, U. M., Platt, J. M., DeMatteo, R. G., Simon, M. C., & Thompson, C. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117773108 · Cited by 975
Targeting Autophagy in Cancer: Recent Advances and Future Directions
Amaravadi, R. K., Kimmelman, A. C., & Debnath, J. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0292 · Cited by 928
Fullerton, M. D., Galic, S., Marcinko, K., Sikkema, S., Pulinilkunnil, T., Chen, Z.-P., O'Neill, H. M., Ford, R. J., Palanivel, R., O'Brien, M., et al. (2013) · Nature Medicine · doi:10.1038/nm.3372 · Cited by 893
Mutant p53 disrupts mammary tissue architecture via the mevalonate pathway
Freed-Pastor, W. A., Mizuno, H., Zhao, X., Langerød, A., Moon, S.-H., Rodriguez-Barrueco, R., Barsotti, A., Chicas, A., Li, W., Polotskaia, A., et al. (2012) · Cell · doi:10.1016/j.cell.2011.12.017 · Cited by 865
Schug, Z. T., Peck, B., Jones, D. T., Zhang, Q., Grosskurth, S., Alam, I. S., Goodwin, L. M., Smethurst, E., Mason, S., Blyth, K., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2014.12.002 · Cited by 820
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792
Aerobic glycolysis promotes T helper 1 cell differentiation through an epigenetic mechanism
Peng, M., Yin, N., Chhangawala, S., Xu, K., Leslie, C. S., & Li, M. O. (2016) · Science · doi:10.1126/science.aaf6284 · Cited by 787
Obesity Shapes Metabolism in the Tumor Microenvironment to Suppress Anti-Tumor Immunity
Ringel, A. E., Drijvers, J. M., Baker, G. J., Catozzi, A., García-Cañaveras, J. C., Gassaway, B. M., Miller, B. C., Juneja, V. R., Nguyen, T. H., Joshi, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.11.009 · Cited by 780
Mitochondrial Metabolism as a Target for Cancer Therapy
Vasan, K., Werner, M., & Chandel, N. S. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.06.019 · Cited by 762
Acetate is a bioenergetic substrate for human glioblastoma and brain metastases
Mashimo, T., Pichumani, K., Vemireddy, V., Hatanpaa, K. J., Singh, D. K., Sirasanagandla, S., Nannepaga, S., Piccirillo, S. G., Kovacs, Z., Foong, C., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.025 · Cited by 760
Neinast, M. D., Murashige, D., & Arany, Z. P. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114455 · Cited by 757
Rysman, E., Brusselmans, K., Scheys, K., Timmermans, L., Derua, R., Munck, S., Veldhoven, P. P. V., Waltregny, D., Daniëls, V. W., Machiels, J., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3871 · Cited by 723
Comerford, S. A., Huang, Z., Du, X., Wang, Y., Cai, L., Witkiewicz, A. K., Walters, H., Tantawy, M. N., Fu, A., Manning, H. C., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.020 · Cited by 681
Mayers, J. R., Wu, C. H., Clish, C. B., Kraft, P. L., Torrence, M. E., Fiske, B. P., Yuan, C., Bao, Y., Townsend, M. K., Tworoger, S. S., et al. (2014) · Nature Medicine · doi:10.1038/nm.3686 · Cited by 672
Sutendra, G., Kinnaird, A. S., Dromparis, P., Paulin, R., Stenson, T. H., Haromy, A., Hashimoto, K., Zhang, N., Flaim, E., & Michelakis, E. D. (2014) · Cell · doi:10.1016/j.cell.2014.04.046 · Cited by 633
Madeo, F., Carmona-Gutierrez, D., Hofer, S. J., & Kroemer, G. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.018 · Cited by 630
Calvisi, D. F., Wang, C., Ho, C., Ladu, S., Lee, S. A., Mattu, S., Destefanis, G., Delogu, S., Zimmermann, A., Ericsson, J., et al. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.12.006 · Cited by 611
Regulation of fatty acid synthesis and oxidation by the AMP-activated protein kinase
Hardie, D. G., & Pan, D. A. (2002) · Biochemical Society Transactions · doi:10.1042/bst0301064 · Cited by 574
Akt-dependent metabolic reprogramming regulates tumor cell histone acetylation
Lee, J. V., Carrer, A., Shah, S., Snyder, N. W., Wei, S., Venneti, S., Worth, A. J., Yuan, Z.-F., Lim, H.-W., Liu, S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.004 · Cited by 563
Dietary fructose feeds hepatic lipogenesis via microbiota-derived acetate
Zhao, S., Jang, C., Liu, J., Uehara, K., Gilbert, M., Izzo, L., Zeng, X., Trefely, S., Fernandez, S., Carrer, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2101-7 · Cited by 553
Self-citationCaloric restriction mimetics enhance anticancer immunosurveillance
Pietrocola, F., Pol, J., Vacchelli, E., Rao, S., Enot, D. P., Baracco, E. E., Levesque, S., Castoldi, F., Jacquelot, N., Yamazaki, T., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.05.016 · Cited by 542
ATP citrate lyase is an important component of cell growth and transformation
Bauer, D. E., Hatzivassiliou, G., Zhao, F., Andreadis, C., & Thompson, C. B. (2005) · Oncogene · doi:10.1038/sj.onc.1208773 · Cited by 537
Svensson, R. U., Parker, S. J., Eichner, L. J., Kolar, M. J., Wallace, M., Brun, S. N., Lombardo, P. S., Van Nostrand, J. L., Hutchins, A., Vera, L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4181 · Cited by 536
Bochet, L., Lehuédé, C., Dauvillier, S., Wang, Y. Y., Dirat, B., Laurent, V., Dray, C., Guiet, R., Maridonneau-Parini, I., Le Gonidec, S., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0530 · Cited by 529
Quantitative Analysis of the Whole-Body Metabolic Fate of Branched-Chain Amino Acids
Neinast, M. D., Jang, C., Hui, S. T., Murashige, D., Chu, Q., Morscher, R. J., Li, X., Zhan, L., White, E., Anthony, T. G., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.10.013 · Cited by 522
GSK-3 as potential target for therapeutic intervention in cancer
McCubrey, J. A., Steelman, L. S., Bertrand, F. E., Davis, N. M., Sokolosky, M. L., Abrams, S. L., Montalto, G., D’Assoro, A. B., Libra, M., Nicoletti, F., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2037 · Cited by 521
Smith, U., & Kahn, B. B. (2016) · Journal of Internal Medicine · doi:10.1111/joim.12540 · Cited by 514
Acetyl-CoA synthetase regulates histone acetylation and hippocampal memory
Mews, P., Donahue, G., Drake, A. M., Luczak, V., Abel, T., & Berger, S. L. (2017) · Nature · doi:10.1038/nature22405 · Cited by 514
Regulation of chromatin and gene expression by metabolic enzymes and metabolites
Li, X., Egervári, G., Wang, Y., Berger, S. L., & Lu, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0029-7 · Cited by 501
Regulation of autophagy by cytosolic acetyl-coenzyme A
Mariño, G., Pietrocola, F., Eisenberg, T., Kong, Y., Malik, S. A., Andryushkova, A., Schroeder, S., Pendl, T., Harger, A., Niso-Santano, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.01.016 · Cited by 500
Pinkosky, S. L., Newton, R. S., Day, E. A., Ford, R. J., Lhotak, S., Austin, R. C., Birch, C. M., Smith, B. K., Filippov, S., Groot, P. H. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms13457 · Cited by 498
Acetate functions as an epigenetic metabolite to promote lipid synthesis under hypoxia
Gao, X. J., Lin, S., Ren, F., Li, J.-T., Chen, J.-J., Yao, C.-B., Yang, H., Jiang, S.-X., Yan, G.-Q., Wang, D., et al. (2016) · Nature Communications · doi:10.1038/ncomms11960 · Cited by 494
Akt-mTORC1 signaling regulates Acly to integrate metabolic input to control of macrophage activation
Covarrubias, A. J., Aksoylar, H., Yu, J., Snyder, N. W., Worth, A. J., Iyer, S. S., Wang, J., Ben‐Sahra, I., Byles, V., Polynne-Stapornkul, T., et al. (2016) · eLife · doi:10.7554/elife.11612 · Cited by 469
Savage, D. B. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27300 · Cited by 447
p53 Represses the Mevalonate Pathway to Mediate Tumor Suppression
Moon, S.-H., Huang, C., Houlihan, S. L., Regunath, K., Freed-Pastor, W. A., Morris, J. P., Tschaharganeh, D. F., Kastenhuber, E. R., Barsotti, A. M., Culp‐Hill, R., et al. (2018) · Cell · doi:10.1016/j.cell.2018.11.011 · Cited by 447
Regulation of acetyl-CoA carboxylase
Brownsey, R. W., Boone, A. N., Elliott, J. E., Kulpa, J. E., & Lee, W. M. (2006) · Biochemical Society Transactions · doi:10.1042/bst20060223 · Cited by 444
Takahashi, H., McCaffery, J. M., Irizarry, R. A., & Boeke, J. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.040 · Cited by 438
Cancer as a Matter of Fat: The Crosstalk between Adipose Tissue and Tumors
Lengyel, E. R., Makowski, L., DiGiovanni, J., & Kolonin, M. G. (2018) · Trends in cancer · doi:10.1016/j.trecan.2018.03.004 · Cited by 436
Squalene accumulation in cholesterol auxotrophic lymphomas prevents oxidative cell death
García‐Bermúdez, J., Baudrier, L., Bayraktar, E. C., Shen, Y., La, K., Guarecuco, R., Yücel, B., Fiore, D., Tavora, B., Freinkman, E., et al. (2019) · Nature · doi:10.1038/s41586-019-0945-5 · Cited by 435
Sugden, M. C., & Holness, M. J. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00526.2002 · Cited by 428
Acetate Production from Glucose and Coupling to Mitochondrial Metabolism in Mammals
Liu, X., Cooper, D. E., Cluntun, A. A., Warmoes, M. O., Zhao, S., Reid, M. A., Liu, J., Lund, P. J., Lopes, M. D. C., Garcia, B. A., et al. (2018) · Cell · doi:10.1016/j.cell.2018.08.040 · Cited by 421
Self-citationKim, C.-W., Addy, C., Kusunoki, J., Anderson, N. N., Deja, S., Fu, X., Burgess, S. C., Li, C., Ruddy, M., Chakravarthy, M., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.07.009 · Cited by 419
Lipogenesis inhibitors: therapeutic opportunities and challenges
Batchuluun, B., Pinkosky, S. L., & Steinberg, G. R. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00367-2 · Cited by 419
Stacpoole, P. W. (2017) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djx071 · Cited by 418
Lally, J., Ghoshal, S., DePeralta, D. K., Moaven, O., Wei, L., Masia, R., Erstad, D. J., Fujiwara, N., Leong, V., Houde, V. P., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.08.020 · Cited by 417
Statins: a repurposed drug to fight cancer
Jiang, W., Hu, J.-W., He, X.-R., Jin, W.-L., & He, X.-Y. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02041-2 · Cited by 417
ATP citrate lyase: activation and therapeutic implications in non-small cell lung cancer
Migita, T., Narita, T., Nomura, K., Miyagi, E., Inazuka, F., Matsuura, M., Ushijima, M., Mashima, T., Seimiya, H., Satoh, Y., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1235 · Cited by 403
Acinar cell plasticity and development of pancreatic ductal adenocarcinoma
Störz, P. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2017.12 · Cited by 401
Important role of the LKB1-AMPK pathway in suppressing tumorigenesis in PTEN-deficient mice
Huang, X., Wullschleger, S., Shpiro, N., McGuire, V. A., Sakamoto, K., Woods, Y. L., Mcburnie, W., Fleming, S., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20080557 · Cited by 396
ATP-citrate lyase controls a glucose-to-acetate metabolic switch
Zhao, S., Torres, A., Henry, R. A., Trefely, S., Wallace, M., Lee, J. V., Carrer, A., Sengupta, A., Campbell, S. L., Kuo, Y.-M., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.069 · Cited by 394
Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth
Lin, R., Tao, R., Gao, X., Li, T., Zhou, X., Guan, K.-L., Xiong, Y., & Lei, Q.-Y. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.002 · Cited by 384
The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
Berwick, D. C., Hers, I., Heesom, K. J., Moule, S. K., & Tavareá, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204681200 · Cited by 383
Nucleus-Translocated ACSS2 Promotes Gene Transcription for Lysosomal Biogenesis and Autophagy
Li, X., Yu, W., Qian, X., Xia, Y., Zheng, Y., Lee, J.-H., Li, W., Lyu, J., Rao, G., Zhang, X., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.026 · Cited by 378
Spatiotemporal Control of Acetyl-CoA Metabolism in Chromatin Regulation
Sivanand, S., Viney, I. A., & Wellen, K. E. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.11.004 · Cited by 374
Self-citationHigh-fructose corn syrup enhances intestinal tumor growth in mice
Goncalves, M. D., Lu, C., Tutnauer, J., Hartman, T. E., Hwang, S.-K., Murphy, C. J., Pauli, C., Morris, R., Taylor, S., Bosch, K., et al. (2019) · Science · doi:10.1126/science.aat8515 · Cited by 374
Fueling the fire: emerging role of the hexosamine biosynthetic pathway in cancer
Akella, N. M., Ciraku, L., & Reginato, M. J. (2019) · BMC Biology · doi:10.1186/s12915-019-0671-3 · Cited by 374
White, P. J., McGarrah, R. W., Grimsrud, P. A., Tso, S.-C., Yang, W.-H., Haldeman, J. M., Grenier-Larouche, T., An, J., Lapworth, A. L., Astapova, I., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.04.015 · Cited by 365
SREBPs in Lipid Metabolism, Insulin Signaling, and Beyond
DeBose‐Boyd, R. A., & Ye, J. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.01.005 · Cited by 363
Nagaraj, R., Sharpley, M. S., Chi, F., Braas, D., Zhou, Y., Kim, R., Clark, A. T., & Banerjee, U. K. (2017) · Cell · doi:10.1016/j.cell.2016.12.026 · Cited by 352
Garcinia cambogia (Hydroxycitric Acid) as a Potential Antiobesity Agent
Heymsfield, S. B., Allison, D. B., Vasselli, J. R., Pietrobelli, A., Greenfield, D., & Nunez, C. (1998) · JAMA · doi:10.1001/jama.280.18.1596 · Cited by 344
Acetate Promotes T Cell Effector Function during Glucose Restriction
Qiu, J., Villa, M., Sanin, D. E., Buck, M. D., O’Sullivan, D., Ching, R., Matsushita, M., Grzes, K. M., Winkler, F., Chang, C.-H., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.022 · Cited by 342
Fructose stimulated de novo lipogenesis is promoted by inflammation
Todoric, J., Di Caro, G., Reibe, S., Henstridge, D. C., Green, C. R., Vrbanac, A., Ceteci, F., Conche, C., McNulty, R., Shalapour, S., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0261-2 · Cited by 328
Low glycaemic diets alter lipid metabolism to influence tumour growth
Lien, E. C., Westermark, A. M., Zhang, Y., Yuan, C., Li, Z., Lau, A. N., Sapp, K. M., Wolpin, B. M., & Heiden, M. G. V. (2021) · Nature · doi:10.1038/s41586-021-04049-2 · Cited by 323
Eight Kinetically Stable but Thermodynamically Activated Molecules that Power Cell Metabolism
Walsh, C. T., Tu, B. P., & Tang, Y. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00510 · Cited by 315
Acetyl-CoA Metabolism Supports Multistep Pancreatic Tumorigenesis
Carrer, A., Trefely, S., Zhao, S., Campbell, S. L., Norgard, R. J., Schultz, K. C., Sidoli, S., Parris, J. L. D., Affronti, H. C., Sivanand, S., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0567 · Cited by 313
Self-citationLiu, M., O’Connor, R. S., Trefely, S., Graham, K. L., Snyder, N. W., & Beatty, G. L. (2019) · Nature Immunology · doi:10.1038/s41590-018-0292-y · Cited by 300
Nuclear Acetyl-CoA Production by ACLY Promotes Homologous Recombination
Sivanand, S., Rhoades, S., Jiang, Q., Lee, J. V., Benci, J., Zhang, J., Yuan, S., Viney, I., Zhao, S., Carrer, A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.008 · Cited by 295
Self-citationLactate supports a metabolic-epigenetic link in macrophage polarization
Noe, J. T., Rendon, B. E., Geller, A. E., Conroy, L. R., Morrissey, S. M., Young, L. E. A., Bruntz, R. C., Kim, E. J., Wise, A. D., Rizzo, M. B. D. S., et al. (2021) · Science Advances · doi:10.1126/sciadv.abi8602 · Cited by 295
Self-citationHarriman, G., Greenwood, J., Bhat, S., Huang, X., Wang, R., Paul, D., Tong, L., Saha, A. K., Westlin, W. F., Kapeller, R., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1520686113 · Cited by 287
García, M. R., Steinbauer, B., Srivastava, K., Singhal, M., Mattijssen, F., Maida, A., Christian, S., Hess‐Stumpp, H., Augustin, H. G., Müller‐Decker, K., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.09.018 · Cited by 281
Brown-fat-mediated tumour suppression by cold-altered global metabolism
Seki, T., Yang, Y., Sun, X., Lim, S., Xie, S., Guo, Z., Xiong, W., Kuroda, M., Sakaue, H., Hosaka, K., et al. (2022) · Nature · doi:10.1038/s41586-022-05030-3 · Cited by 277
Compartmentalised acyl-CoA metabolism and roles in chromatin regulation
Trefely, S., Lovell, C. D., Snyder, N. W., & Wellen, K. E. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.01.005 · Cited by 272
Self-citationNAFLD‐related hepatocellular carcinoma: The growing challenge
Shah, P. A., Patil, R., & Harrison, S. A. (2022) · Hepatology · doi:10.1002/hep.32542 · Cited by 270
Tricarballylate and hydroxycitrate: Substrate and inhibitor of ATP: Citrate oxaloacetate lyase
Watson, J. A., Fang, M., & Lowenstein, J. M. (1969) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(69)90532-3 · Cited by 268
Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal
Abu-Elheiga, L. A., Matzuk, M. M., Kordari, P., Oh, W. K., Shaiken, T. E., Gu, Z., & Wakil, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505714102 · Cited by 266
Bulusu, V., Tumanov, S., Michalopoulou, E., van den Broek, N. J. F., Mackay, G., Nixon, C., Dhayade, S., Schug, Z. T., Voorde, J. V., Blyth, K., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.055 · Cited by 263
Chemistry and Biochemistry of (−)-Hydroxycitric Acid from Garcinia
Jena, B. S., Jayaprakasha, G. K., Singh, R. P., & Sakariah, K. K. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf010753k · Cited by 259
Energy status dictates PD-L1 protein abundance and anti-tumor immunity to enable checkpoint blockade
Dai, X., Bu, X., Gao, Y., Guo, J., Hu, J., Jiang, C., Zhang, Z., Xu, K., Duan, J., He, S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.037 · Cited by 257
BCAT2-mediated BCAA catabolism is critical for development of pancreatic ductal adenocarcinoma
Li, J., Yin, M., Wang, D., Wang, J., Lei, M., Zhang, Y., Liu, Y., Zhang, L., Zou, S., Hu, L.-P., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-019-0455-6 · Cited by 248
He, A., Chen, X., Tan, M., Chen, Y., Lu, D., Zhang, X., Dean, J. M., Razani, B., & Lodhi, I. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.05.007 · Cited by 243
Pinkosky, S. L., Filippov, S. I., Srivastava, R. A. K., Hanselman, J. C., Bradshaw, C. D., Hurley, T. R., Cramer, C. T., Spahr, M. A., Brant, A. F., Houghton, J. L., et al. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m030528 · Cited by 241
Wang, Q. A., Jiang, L., Wang, J., Li, S., Yu, Y., You, J., Zeng, R., Gao, X., Rui, L., Li, W., et al. (2008) · Hepatology · doi:10.1002/hep.22774 · Cited by 215
Regulator of Fatty Acid Metabolism, Acetyl Coenzyme A Carboxylase 1, Controls T Cell Immunity
Lee, J., Walsh, M. C., Hoehn, K. L., James, D. E., Wherry, E. J., & Choi, Y. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302985 · Cited by 215
Kondo, A., Yamamoto, S., Nakaki, R., Shimamura, T., Hamakubo, T., Sakai, J., Kodama, T., Yoshida, T., Aburatani, H., & Osawa, T. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.006 · Cited by 205
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle
Verschueren, K. H. G., Blanchet, C. E., Félix, J., Dansercoer, A., Vos, D. E. D., Bloch, Y., BEEUMEN, J. V., Svergun, D. I., Gutsche, I., Savvides, S. N., et al. (2019) · Nature · doi:10.1038/s41586-019-1095-5 · Cited by 205
Chen, J., Guccini, I., Mitri, D. D., Brina, D., Revandkar, A., Sarti, M., Pasquini, E., Alajati, A., Pinton, S., Losa, M., et al. (2018) · Nature Genetics · doi:10.1038/s41588-017-0026-3 · Cited by 202
Inhibition of ATP-citrate lyase improves NASH, liver fibrosis, and dyslipidemia
Morrow, M. R., Batchuluun, B., Wu, J., Ahmadi, E., Leroux, J. M., Mohammadi-Shemirani, P., Desjardins, E. M., Wang, Z., Tsakiridis, E. E., Lavoie, D. C. T., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.05.004 · Cited by 199
Statins as Anticancer Agents in the Era of Precision Medicine
Longo, J., van Leeuwen, J. E., Elbaz, M., Branchard, E., & Penn, L. Z. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-1967 · Cited by 196
USP22 regulates lipidome accumulation by stabilizing PPARγ in hepatocellular carcinoma
Ning, Z., Guo, X., Liu, X., Lu, C., Wang, A., Wang, X., Wang, W., Chen, H., Qin, W., Liu, X., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29846-9 · Cited by 196
Gouw, A. M., Margulis, K., Liu, N. S., Raman, S. J., Mancuso, A., Toal, G. G., Tong, L., Mosley, A. R., Hsieh, A. L., Sullivan, D. K., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.07.012 · Cited by 195
Metabolic Signaling to the Nucleus in Cancer
Campbell, S. L., & Wellen, K. E. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.015 · Cited by 186
Self-citationAn allosteric mechanism for potent inhibition of human ATP-citrate lyase
Jia, W., Leit, S. M., Kuai, J., Therrien, É., Rafi, S. B., Harwood, H. J., DeLaBarre, B., & Tong, L. (2019) · Nature · doi:10.1038/s41586-019-1094-6 · Cited by 186
Potapova, I. A., El‐Maghrabi, M. R., Doronin, S. V., & Benjamin, W. B. (2000) · Biochemistry · doi:10.1021/bi992159y · Cited by 176
Alkhouri, N., Lawitz, E., Noureddin, M., DeFronzo, R., & Shulman, G. I. (2020) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2020.1668374 · Cited by 162
mTORC2-AKT signaling to ATP-citrate lyase drives brown adipogenesis and de novo lipogenesis
Calejman, C. M., Trefely, S., Entwisle, S. W., Luciano, A. K., Jung, S., Hsiao, W., Torres, A., Hung, C. M., Li, H., Snyder, N. W., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14430-w · Cited by 161
Self-citationHuang, Z., Zhang, M., Plec, A. A., Estill, S. J., Cai, L., Repa, J. J., McKnight, S. L., & Tu, B. P. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806635115 · Cited by 160
PHD3 Loss in Cancer Enables Metabolic Reliance on Fatty Acid Oxidation via Deactivation of ACC2
German, N. J., Yoon, H., Yusuf, R. Z., Murphy, J. P., Finley, L. W. S., Laurent, G., Haas, W., Satterstrom, F. K., Guarnerio, J., Zaganjor, E., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.014 · Cited by 156
Sustained SREBP-1-dependent lipogenesis as a key mediator of resistance to BRAF-targeted therapy
Talebi, A., Dehairs, J., Rambow, F., Rogiers, A., Nittner, D., Derua, R., Vanderhoydonc, F., Duarte, J. A. G., Bosisio, F., Van den Eynde, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04664-0 · Cited by 155
ATP-Citrate Lyase Deficiency in the Mouse
Beigneux, A. P., Kosinski, C., Gavino, B. J., Horton, J. D., Skarnes, W. C., & Young, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310512200 · Cited by 154
Lipid Metabolism in Development and Progression of Hepatocellular Carcinoma
Sangineto, M., Villani, R., Cavallone, F., Romano, A. D., Loizzi, D., & Serviddio, G. (2020) · Cancers · doi:10.3390/cancers12061419 · Cited by 153
Macrophages are metabolically heterogeneous within the tumor microenvironment
Geeraerts, X., Fernández-García, J., Hartmann, F. J., de Goede, K. E., Martens, L., Elkrim, Y., Debraekeleer, A., Stijlemans, B., Vandekeere, A., Rinaldi, G., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110171 · Cited by 151
Lü, M., Zhu, W., Wang, X., Tang, J.-J., Zhang, K., Yu, G., Shao, W., Lin, Z., Wang, S.-H., Lu, L., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2018.12.019 · Cited by 150
Mitochondrial acetylcarnitine provides acetyl groups for nuclear histone acetylation
Madiraju, P., Pande, S. V., Prentki, M., & Madiraju, S. R. M. (2009) · Epigenetics · doi:10.4161/epi.4.6.9767 · Cited by 147
The IKKβ‐USP30‐ACLY Axis Controls Lipogenesis and Tumorigenesis
Gu, L., Zhu, Y., Lin, X., Lu, B., Zhou, X., Zhou, F., Zhao, Q., Prochownik, E. V., & Li, Y. (2020) · Hepatology · doi:10.1002/hep.31249 · Cited by 147
Long-chain fatty acyl-CoA esters regulate metabolism via allosteric control of AMPK β1 isoforms
Pinkosky, S. L., Scott, J. W., Desjardins, E. M., Smith, B. K., Day, E. A., Ford, R. J., Langendorf, C. G., Ling, N. X. Y., Nero, T. L., Loh, K., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0245-2 · Cited by 145
The role of ATP citrate-lyase in the metabolic regulation of plasma lipids
PEARCE, N. J., Yates, J. W., Berkhout, T. A., Jackson, B., Tew, D. G., Boyd, H., Camilleri, P., Sweeney, P. J., Gribble, A. D., Shaw, A. N., et al. (1998) · Biochemical Journal · doi:10.1042/bj3340113 · Cited by 144
Onakpoya, I., Hung, S. K., Perry, R. E., Wider, B., & Ernst, E. (2010) · Journal of Obesity · doi:10.1155/2011/509038 · Cited by 143
Sink into the Epigenome: Histones as Repositories That Influence Cellular Metabolism
Ye, C., & Tu, B. P. (2018) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.06.002 · Cited by 142
Zhang, C., Liu, J., Huang, G., Zhao, Y., Yue, X., Wu, H., Li, J., Zhu, J., Shen, Z., Haffty, B. G., et al. (2016) · Genes & Development · doi:10.1101/gad.283283.116 · Cited by 140
Quantitative Sub-Cellular Acyl-Coa Analysis Reveals Distinct Nuclear Regulation
Trefely, S., Huber, K., Liu, J., Noji, M., Stransky, S., Singh, J. P., Doan, M. T., Lovell, C. D., von Krusenstiern, E. V., Jiang, H., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.11.006 · Cited by 139
Self-citationMacrophage ATP citrate lyase deficiency stabilizes atherosclerotic plaques
Baardman, J., Verberk, S. G. S., van der Velden, S., Gijbels, M. J., van Roomen, C. P. A. A., Sluimer, J. C., Broos, J. Y., Griffith, G. R., Prange, K. H. M., van Weeghel, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-20141-z · Cited by 134
Self-citationHepatic De Novo Lipogenesis Is Present in Liver-Specific ACC1-Deficient Mice
Harada, N., Oda, Z., Hara, Y., Fujinami, K., Okawa, M., Ohbuchi, K., Yonemoto, M., Ikeda, Y., Ohwaki, K., Aragane, K., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01122-06 · Cited by 132
Older than genes: the acetyl CoA pathway and origins
Martin, W. F. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00817 · Cited by 132 · cited 1×
“Specific cancer genetic alterations have been shown to promote mevalonate pathway dependence, including TP53 loss in HCC, TP53 mutation in breast cancer and t(4;14) chromosomal translocation in multiple myeloma.”
BackgroundSerine catabolism generates liver NADPH and supports hepatic lipogenesis
Zhang, Z., TeSlaa, T. A., Xu, X., Zeng, X., Yang, L., Xing, G., Tesz, G. J., Clasquin, M. F., & Rabinowitz, J. D. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00487-4 · Cited by 130
Pomatto, L. C. D., Bodogai, M., Bosompra, O., Kato, J. I., Wong, S., Carpenter, M., Duregon, E., Chowdhury, D., Krishna, P., Ng, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26431-4 · Cited by 126
Acetyl-CoA promotes glioblastoma cell adhesion and migration through Ca 2+ –NFAT signalingPreprint
Lee, J. V., Berry, C. T., Kim, K., Sen, P., Kim, T., Carrer, A., Trefely, S., Zhao, S., Fernandez, S., Barney, L. E., et al. (2018) · Genes & Development · doi:10.1101/gad.311027.117 · Cited by 121
Self-citationLactate is an epigenetic metabolite that drives survival in model systems of glioblastoma
Torrini, C., Nguyen, T. T. T., Shu, C., Mela, A., Humala, N., Mahajan, A., Seeley, E., Zhang, G., Westhoff, M., Karpel‐Massler, G., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.06.030 · Cited by 117
McGregor, G. H., Campbell, A. D., Fey, S. K., Tumanov, S., Sumpton, D. P., Blanco, G. R., Mackay, G., Nixon, C., Vázquez, A., Sansom, O. J., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0644 · Cited by 116
Cancer‐associated adipocytes promote pancreatic cancer progression through SAA1 expression
Takehara, M., Sato, Y., Kimura, T., Noda, K., Miyamoto, H., Fujino, Y., Miyoshi, J., Nakamura, F., Wada, H., Bando, Y., et al. (2020) · Cancer Science · doi:10.1111/cas.14527 · Cited by 115
Hughes, K., Ramakrishna, S., Benjamin, W. B., & Woodgett, J. R. (1992) · Biochemical Journal · doi:10.1042/bj2880309 · Cited by 113
Chow, J. D. Y., Lawrence, R., Healy, M. E., Dominy, J. E., Liao, J. A., Breen, D. S., Byrne, F. L., Kenwood, B. M., Lackner, C., Okutsu, S., et al. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.02.004 · Cited by 111
Acetyl-CoA Synthetase 2: A Critical Linkage in Obesity-Induced Tumorigenesis in Myeloma
Li, Z., Liu, H., He, J., Wang, Z., Yin, Z., You, G., Wang, Z., Davis, R. E., Lin, P., Bergsagel, P. L., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2020.12.011 · Cited by 110
Pandyra, A. A., Mullen, P., Kalkat, M., Yu, R., Pong, J. T., Li, Z., Trudel, S., Lang, K. S., Minden, M. D., Schimmer, A. D., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0130 · Cited by 109
AT-1 is the ER membrane acetyl-CoA transporter and is essential for cell viability
Jonas, M. C., Pehar, M., & Puglielli, L. (2010) · Journal of Cell Science · doi:10.1242/jcs.068841 · Cited by 108
Kim, C.-W., Addy, C., Kusunoki, J., Anderson, N. N., Deja, S., Fu, X., Burgess, S. C., Cai, L., Ruddy, M., Chakravarthy, M. V., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.011 · Cited by 105
Targeting ACSS2 with a Transition-State Mimetic Inhibits Triple-Negative Breast Cancer Growth
Miller, K. D., Pniewski, K. A., Perry, C. E., Papp, S. B., Shaffer, J. D., Velasco‐Silva, J. N., Casciano, J. C., Aramburu, T. M., Srikanth, Y. V. V., Cassel, J. A., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-1847 · Cited by 103
An actionable sterol-regulated feedback loop modulates statin sensitivity in prostate cancer
Longo, J., Mullen, P., Yu, R., van Leeuwen, J. E., Masoomian, M., Woon, D. T. S., Wang, Y. Z., Chen, E. X., Hamilton, R. J., Sweet, J., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.04.003 · Cited by 100
Adipocyte mesenchymal transition contributes to mammary tumor progression
Zhu, Q., Zhu, Y., Hepler, C., Zhang, Q., Park, J., Gliniak, C. M., Henry, G. H., Crewe, C., Bu, D., Zhang, Z., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111362 · Cited by 99
Nelson, M. E., Lahiri, S., Chow, J. D. Y., Byrne, F. L., Hargett, S. R., Breen, D. S., Olzomer, E. M., Wu, L. E., Cooney, G. J., Turner, N. A., et al. (2017) · Nature Communications · doi:10.1038/ncomms14689 · Cited by 93
ATP-citrate lyase: genetics, molecular biology and therapeutic target for dyslipidemia
Burke, A. C., & Huff, M. W. (2017) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000390 · Cited by 91
Incorporation of radioactive citrate into fatty acids
Srere, P. A., & Bhaduri, A. (1962) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(62)90205-6 · Cited by 87 · cited 1×
“Specific cancer genetic alterations have been shown to promote mevalonate pathway dependence, including TP53 loss in HCC, TP53 mutation in breast cancer and t(4;14) chromosomal translocation in multiple myeloma.”
BackgroundACSS2-mediated acetyl-CoA synthesis from acetate is necessary for human cytomegalovirus infection
Vysochan, A., Sengupta, A., Weljie, A. M., Alwine, J. C., & Yu, Y. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614268114 · Cited by 86
Nature and Nurture: What Determines Tumor Metabolic Phenotypes?
Mayers, J. R., & Heiden, M. G. V. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0165 · Cited by 86
The incorporation of citrate carbon into fatty acids
Bhaduri, A., & Srere, P. A. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)90747-9 · Cited by 85
Shah, S., Carriveau, W. J., Li, J., Campbell, S. L., Kopinski, P. K., Lim, H., Daurio, N. A., Trefely, S., Won, K., Wallace, D. C., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9666 · Cited by 85
Self-citationFat Induces Glucose Metabolism in Nontransformed Liver Cells and Promotes Liver Tumorigenesis
Broadfield, L. A., Duarte, J. A. G., Schmieder, R., Broekaert, D., Veys, K., Planque, M., Vriens, K., Karasawa, Y., Napolitano, F., Fujita, S., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-1954 · Cited by 85
Fernandez, S., Viola, J. M., Torres, A., Wallace, M., Trefely, S., Zhao, S., Affronti, H. C., Gengatharan, J. M., Guertin, D. A., Snyder, N. W., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.112 · Cited by 80
Self-citationZervopoulos, S. D., Boukouris, A. E., Saleme, B., Haromy, A., Tejay, S., Sutendra, G., & Michelakis, E. D. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.02.003 · Cited by 75
Guy, P. S., Cohen, P., & Hardie, D. G. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05160.x · Cited by 73
Qiao, C., Huang, W., Chen, J., Feng, W., Zhang, T., Wang, Y., Liu, D., Ji, X., Xie, M., Sun, M., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03833-2 · Cited by 71
Enzymatic transfer of acetate on histones from lysine reservoir sites to lysine activating sites
Mendoza, M. R., Egervári, G., Sidoli, S., Donahue, G., Alexander, D. C., Sen, P., Garcia, B. A., & Berger, S. L. (2022) · Science Advances · doi:10.1126/sciadv.abj5688 · Cited by 65
The Bidirectional Relationship Between Cancer Epigenetics and Metabolism
Izzo, L., Affronti, H. C., & Wellen, K. E. (2020) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-070820-035832 · Cited by 64
Self-citationIn vivo isotope tracing reveals the versatility of glucose as a brown adipose tissue substrate
Jung, S. M., Doxsey, W. G., Le, J., Haley, J. D., Mazuecos, L., Luciano, A. K., Li, H., Jang, C., & Guertin, D. A. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109459 · Cited by 63
Self-citationWei, X., Shi, J., Lin, Q., Ma, X., Pang, Y., Mao, H., Li, R., Lü, W., Wang, Y., & Liu, P. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.642229 · Cited by 60
NaCT/SLC13A5 facilitates citrate import and metabolism under nutrient-limited conditions
Kumar, A., Cordes, T., Thalacker‐Mercer, A. E., Pajor, A. M., Murphy, A. N., & Metallo, C. M. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109701 · Cited by 60
Ciraku, L., Bacigalupa, Z. A., Ju, J., Moeller, R. A., Minh, G. L., Lee, R. H., Smith, M. D., Ferrer, C. M., Trefely, S., Izzo, L., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02237-6 · Cited by 60
Self-citationMolecular basis for acetyl-CoA production by ATP-citrate lyase
Wei, X., Schultz, K. C., Bazilevsky, G. A., Vogt, A. D., & Marmorstein, R. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0351-6 · Cited by 58
Intracellular Acetyl CoA Potentiates the Therapeutic Efficacy of Antitumor CD8+ T Cells
Chowdhury, S., Kar, A., Bhowmik, D., Gautam, A., Basak, D., Sarkar, I., Ghosh, P., Sarkar, D., Deka, A., Chakraborty, P., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-4052 · Cited by 58
Dieterich, I. A., Lawton, A. J., Peng, Y., Yu, Q., Rhoads, T. W., Overmyer, K. A., Cui, Y., Armstrong, E. A., Howell, P. R., Burhans, M. S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11945-9 · Cited by 55
ACLY: A biomarker of recurrence in breast cancer
Chen, Y., Li, K., Gong, D., Zhang, J., Li, Q., Zhao, G., & Lin, P. (2020) · Pathology - Research and Practice · doi:10.1016/j.prp.2020.153076 · Cited by 53
Zheng, Y., Zhou, Q., Zhao, C., Li, J., Yu, Z., & Zhu, Q. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16235 · Cited by 53
Huber, K., Hofer, D., Trefely, S., Pelzmann, H. J., Madreiter‐Sokolowski, C. T., Duta-Mare, M., Schlager, S., Trausinger, G., Stryeck, S., Graier, W. F., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.08.017 · Cited by 49
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Montgomery, D. C., Garlick, J. M., Kulkarni, R. A., Kennedy, S., Allali‐Hassani, A., Kuo, Y., Andrews, A. J., Wu, H., Vedadi, M., & Meier, J. L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03036 · Cited by 48
Wellen, K. E., & Snyder, N. W. (2019) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000580 · Cited by 48
Self-citationSun, L., Kong, Y., Cao, M., Zhou, H., Li, H., Cui, Y., Fang, F., Zhang, W., Li, J., Zhu, X., et al. (2017) · Cancer Science · doi:10.1111/cas.13252 · Cited by 47
Bae, J. M., Kim, J. H., Oh, H. J., Park, H. E., Lee, T. H., Cho, N., & Kang, G. H. (2016) · Modern Pathology · doi:10.1038/modpathol.2016.172 · Cited by 44
Low expression of ACLY associates with favorable prognosis in acute myeloid leukemia
Wang, J., Ye, W., Yan, X., Guo, Q., Ma, Q., Lin, F., Huang, J., & Jin, J. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-1884-5 · Cited by 43
Hyperinsulinemia promotes aberrant histone acetylation in triple-negative breast cancer
Senapati, P., Kato, H., Lee, M., Leung, A., Thai, C., Sanchez, A., Gallagher, E. J., LeRoith, D., Seewaldt, V. L., Ann, D. K., et al. (2019) · Epigenetics & Chromatin · doi:10.1186/s13072-019-0290-9 · Cited by 43
Allosteric regulation of the biotin-dependent enzyme pyruvate carboxylase by acetyl-CoA
Adina-Zada, A., Zeczycki, T. N., Maurice, M. S., Jitrapakdee, S., Cleland, W. W., & Attwood, P. V. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120041 · Cited by 42
AMPK β1 reduces tumor progression and improves survival in p53 null mice
Houde, V. P., Donzelli, S., Sacconi, A., Galić, S., Hammill, J. A., Bramson, J. L., Foster, R. A., Tsakiridis, T. K., Kemp, B. E., Grasso, G., et al. (2017) · Molecular Oncology · doi:10.1002/1878-0261.12079 · Cited by 41
Rat mammary gland ATP‐citrate lyase is phosphorylated by cyclic AMP‐dependent protein kinase
Guy, P. S., Cohen, P., & Hardie, D. G. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)81087-8 · Cited by 38
Advances into understanding metabolites as signaling molecules in cancer progression
Liu, J. Y., & Wellen, K. E. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.01.013 · Cited by 38
Self-citationPark, G. S. H., Jung, S., Wellen, K. E., & Jang, C. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00614-x · Cited by 37
Self-citationYenilmez, B., Kelly, M., Zhang, G., Wetoska, N., Ilkayeva, O., Min, K., Rowland, L. A., DiMarzio, C., He, W., Raymond, N., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102401 · Cited by 36
The mevalonate pathway is an actionable vulnerability of t(4;14)-positive multiple myeloma
Longo, J., Smirnov, P., Li, Z., Branchard, E., van Leeuwen, J. E., Licht, J. D., Haibe‐Kains, B., Andrews, D. W., Keats, J. J., Pugh, T. J., et al. (2020) · Leukemia · doi:10.1038/s41375-020-0962-2 · Cited by 33
Zhang, S., He, J., Jia, Z., Yan, Z., & Yang, J. (2018) · Urologic Oncology Seminars and Original Investigations · doi:10.1016/j.urolonc.2018.01.013 · Cited by 31
Trefely, S., Liu, J., Huber, K., Doan, M. T., Jiang, H., Singh, J. P., von Krusenstiern, E. V., Bostwick, A., Xu, P. J., Bogner‐Strauß, J. G., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.09.004 · Cited by 28
Self-citationA Systems Chemoproteomic Analysis of Acyl-CoA/Protein Interaction Networks
Levy, M. J., Montgomery, D. C., Sardiu, M. E., Montaño, J. L., Bergholtz, S. E., Nance, K. D., Thorpe, A. L., Fox, S. D., Lin, Q., Andrésson, Þ., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.011 · Cited by 27
Comparison of phospho- and dephospho-ATP citrate lyase
Ranganathan, N. S., Srere, P. A., & Linn, T. C. (1980) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(80)90006-5 · Cited by 26
ACLY is the Novel Signaling Target of PIP 2/PIP 3 and Lyn in Cancer
Basappa, J., Citir, M., Zhang, Q., Wang, H. Y., Liu, X., Melnikov, O., Yahya, H. A., Stein, F., Müller, R., Traynor‐Kaplan, A., et al. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e03910 · Cited by 26
Effects of phosphorylation on the kinetic properties of rat liver ATP-citrate lyase
Houston, B., & Nimmo, H. G. (1985) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(85)90095-3 · Cited by 24
Structure of ACLY in complex with CoA
Wei, X., & Marmorstein, R. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6poe/pdb · Cited by 24
Effect of Oxaloacetate and Phosphorylation on ATP-Citrate Lyase Activity
Pentyala, S., & Benjamin, W. B. (1995) · Biochemistry · doi:10.1021/bi00035a001 · Cited by 20
Xu, Y., Zhang, Z., Xu, D., Yang, X. L., Zhou, L., & Zhu, Y. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02108-2 · Cited by 20
Odera, J. O., Xiong, Z., Huang, C. D., Gu, N., Yang, W., Githanga, J. N., Odera, E. O., Paiboonrungruang, C., & Chen, X. L. (2020) · Biochemical Journal · doi:10.1042/bcj20200452 · Cited by 16
Metabolic convergence on lipogenesis in RAS, BCR-ABL, and MYC-driven lymphoid malignancies
Liefwalker, D. F., Gabay, M., Wang, Z., Pathak, K. V., Plaisier, S. B., Shah, V. M., Babra, B., Dewson, G. S., Lai, I. K., Mosley, A. R., et al. (2021) · Cancer & Metabolism · doi:10.1186/s40170-021-00263-8 · Cited by 12
de Goede, K. E., Verberk, S. G. S., Baardman, J., Harber, K. J., van Kooyk, Y., de Winther, M. P. J., Schetters, S. T. T., & den Bossche, J. V. (2021) · Cancers · doi:10.3390/cancers13123054 · Cited by 10
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Metadata
- Authors
- Guertin, D. A., & Wellen, K. E.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- University of Pennsylvania (US)
- Corresponding author
- Guertin, David A.
- Wellen, Kathryn E.
- Venue
- Nature Reviews Cancer
- Published
- 2023-01-19
- Volume
- 23
- Issue
- 3
- Pages
- 156-172
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- PMC
- PMC11137663
- OpenAlex
- W4317436153
- Cited by
- 303
- References
- 200
- Citations by year
- 2026: 85 · 2025: 120 · 2024: 69 · 2023: 29
- FWCI
- 9.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature reviews. Cancer (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- Funders
- National Institutes of Health
- National Cancer Institute (R01CA174761, R01CA248315, R01CA228339, R01CA262055)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK094004, R01DK116005, R01DK127175)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- acetyl-CoA metabolism, cancer metabolism, TCA cycle, fatty acid synthesis, isoprenoid biosynthesis, lysine acetylation, protein acetylation, metabolic signalling, stable isotope tracing
- MeSH terms
- Acetyl Coenzyme A, Animals, Disease Models, Animal, Humans, Neoplasms, Mice, Metabolic Networks and Pathways
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