Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12 provides a tertiary level of regulation of fatty acid synthesis
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Acetyl-CoA carboxylase (ACC), the first committed enzyme in fatty acid (FA) synthesis, is regulated by phosphorylation/dephosphorylation, transcription, and an unusual mechanism of protein polymerization. Polymerization of ACC increases enzymatic activity and is induced in vitro by supraphysiological concentrations of citrate (> 5 mM). Here, we show that MIG12, a 22 kDa cytosolic protein of previously unknown function, binds to ACC and lowers the threshold for citrate activation into the physiological range (< 1 mM). In vitro, recombinant MIG12 induced polymerization of ACC (as determined by nondenaturing gels, FPLC, and electron microscopy) and increased ACC activity by > 50-fold in the presence of 1 mM citrate. In vivo, overexpression of MIG12 in liver induced ACC polymerization, increased FA synthesis, and produced triglyceride accumulation and fatty liver. Thus, in addition to its regulation by phosphorylation and transcription, ACC is regulated at a tertiary level by MIG12, which facilitates ACC polymerization and enhances enzymatic activity.
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Cytosolic citrate is a potent allosteric regulator of ACC by increasing its polymerization and activity.
“Cytosolic citrate is a potent allosteric regulator of ACC by increasing its polymerization and activity.83”
From The multifaceted contributions of mitochondria to cellular metabolism (2018) · cites this paper as [83]
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SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15593 · Cited by 4,285 · see citing works
Self-citationSREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215593 · Cited by 4,092 · see citing works
Self-citationKahn, B. B., Alquier, T., Carling, D., & Hardie, D. G. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.003 · Cited by 2,799 · see citing works
Horton, J. D., Shah, N. A., Warrington, J. A., Anderson, N. N., Park, S. W., Brown, M. S., & Goldstein, J. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1534923100 · Cited by 1,427 · see citing works
Self-citationIntegration of metabolism and inflammation by lipid-activated nuclear receptors
Bensinger, S. J., & Tontonoz, P. (2008) · Nature · doi:10.1038/nature07202 · Cited by 813 · see citing works
Shimano, H., Horton, J. D., Hammer, R. E., Shimomura, I., Brown, M. S., & Goldstein, J. L. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118951 · Cited by 810 · see citing works
Self-citationJoseph, 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 779 · see citing works
A possible role for malonyl-CoA in the regulation of hepatic fatty acid oxidation and ketogenesis.
McGarry, J. D., Mannaerts, G. P., & Foster, D. W. (1977) · Journal of Clinical Investigation · doi:10.1172/jci108764 · Cited by 736 · see citing works
Fatty acid metabolism: Target for metabolic syndrome
Wakil, S. J., & Abu-Elheiga, L. A. (2009) · Journal of Lipid Research · doi:10.1194/jlr.r800079-jlr200 · Cited by 731 · see citing works
Regulation of sterol regulatory element binding proteins in livers of fasted and refed mice
Horton, J. D., Bashmakov, Y. K., Shimomura, I., & Shimano, H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5987 · Cited by 669 · see citing works
Self-citationChen, 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 546 · see citing works
Identification of a Physiologically Relevant Endogenous Ligand for PPARα in Liver
Chakravarthy, M. V., Lodhi, I. J., Yin, L., Malapaka, R. R. V., Xu, H. E., TURK, J. W., & Semenkovich, C. F. (2009) · Cell · doi:10.1016/j.cell.2009.05.036 · Cited by 534 · see citing works
The subcellular localization of acetyl-CoA carboxylase 2
Abu-Elheiga, L. A., Brinkley, W. R., Zhong, L., Chirala, S. S., Woldegiorgis, G., & Wakil, S. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1444 · Cited by 450 · see citing works
Carbohydrate response element binding protein directly promotes lipogenic enzyme gene transcription
Ishii, S., Iizuka, K., Miller, B. C., & Uyeda, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405238101 · Cited by 416 · see citing works
Evidence for the participation of biotin in the enzymic synthesis of fatty acids
Wakil, S. J., Titchener, E. B., & Gibson, D. M. (1958) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(58)90177-x · Cited by 306 · see citing works
Brookheart, R. T., Michel, C. I., & Schaffer, J. E. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.011 · Cited by 279 · see citing works
Engelking, L. J., Kuriyama, H., Hammer, R. E., Horton, J. D., Brown, M. S., Goldstein, J. L., & Liang, G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20978 · Cited by 273 · see citing works
Self-citationIdentification of an isozymic form of acetyl-CoA carboxylase.
Bianchi, A., Evans, J. L., Iverson, A. J., Nordlund, A. C., Watts, T. D., & Witters, L. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40045-8 · Cited by 261 · see citing works
Deletion of ELOVL5 leads to fatty liver through activation of SREBP-1c in mice
Moon, Y.-A., Hammer, R. E., & Horton, J. D. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800383-jlr200 · Cited by 237 · see citing works
Self-citationIizuka, K., Miller, B., & Uyeda, K. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00027.2006 · Cited by 195 · see citing works
Formation of malonyl coenzyme A in rat heart
Thampy, K. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84614-8 · Cited by 153 · see citing works
Molecular characteristics of liver acetyl CoA carboxylase.
Gregolin, C., Ryder, E., Kleinschmidt, A. K., Warner, R. C., & Lane, M. D. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.56.1.148 · Cited by 133 · see citing works
Insulin stimulates the dephosphorylation and activation of acetyl-CoA carboxylase.
Witters, L. A., Watts, T. D., Daniels, D., & Evans, J. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.15.5473 · Cited by 114 · see citing works
The Spot 14 Protein Is Required for de Novo Lipid Synthesis in the Lactating Mammary Gland
Zhu, Q., Anderson, G. W., Mucha, G. T., Parks, E. J., Metkowski, J. K., & Mariash, C. N. (2005) · Endocrinology · doi:10.1210/en.2005-0204 · Cited by 95 · see citing works
Activation of acetyl-CoA carboxylase. Purification and properties of a Mn2+-dependent phosphatase.
Thampy, K. G., & Wakil, S. J. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88973-6 · Cited by 85 · see citing works
Thampy, K. G., & Wakil, S. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68807-6 · Cited by 77 · see citing works
Berti, C., Fontanella, B., Ferrentino, R., & Meroni, G. (2004) · BMC Cell Biology · doi:10.1186/1471-2121-5-9 · Cited by 73 · see citing works
Cheng, D., Chu, C.-H., Chen, L., Feder, J. N., Mintier, G. A., Wu, Y., Cook, J. W., Harpel, M. R., Locke, G. A., An, Y., et al. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.06.005 · Cited by 53 · see citing works
Self-citationRoss, K. L., & Eisenstein, R. S. (2002) · Journal of Nutrition · doi:10.1093/jn/132.4.643 · Cited by 30 · see citing works
Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics
Kaushik, V. K., Kavana, M., Volz, J. M., Weldon, S. C., Hanrahan, S., Xu, J., Caplan, S. L., & Hubbard, B. K. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.02.004 · Cited by 14 · see citing works
Transient up-regulation of a novel member of Spot 14 family in androgen-stimulated rat prostate
Nishi, N., SHOJI, H., Miyanaka, H., & NAKAMURA, T. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.05.001 · Cited by 8 · see citing works
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Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935 · see citing works
Nonalcoholic fatty liver disease as a nexus of metabolic and hepatic diseases
Samuel, V. T., & Shulman, G. I. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.002 · Cited by 745 · see citing works
“2016), and protein-protein interaction (MIG-12-mediated polymerization of ACC enhances activity) (Kim et al., 2010).”
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Sanders, F., & Griffin, J. L. (2015) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12178 · Cited by 543 · see citing works
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Knobloch, M., Braun, S., Zurkirchen, L., Schoultz, C., Zamboni, N., Araúzo-Bravo, M., Kovacs, W. J., Karalay, Ö., Suter, U., Machado, R. A. C., et al. (2012) · Nature · doi:10.1038/nature11689 · Cited by 503 · see citing works
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Tong, L. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1096-0 · Cited by 473 · see citing works
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Bauman, D. E., Harvatine, K. J., & Lock, A. L. (2011) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104648 · Cited by 318 · see citing works
Structural basis for regulation of human acetyl-CoA carboxylase
Hunkeler, M., Hagmann, A., Stuttfeld, E., Chami, M., Guri, Y., Stahlberg, H., & Maier, T. (2018) · Nature · doi:10.1038/s41586-018-0201-4 · Cited by 229 · see citing works
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Galdieri, L. C., & Vančura, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380519 · Cited by 223 · see citing works
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Krueger, F., Parasuraman, R., Iyengar, V., Thornburg, M., Weel, J., Lin, M., Clarke, E., McCabe, K., & Lipsky, R. H. (2012) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2012.00004 · Cited by 207 · see citing works
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Urrutia, N. L., & Harvatine, K. J. (2017) · Journal of Nutrition · doi:10.3945/jn.116.245001 · Cited by 183 · see citing works
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 · see citing works
Zhu, Z., Hu, Y., Teixeira, P. G., Pereira, R., Chen, Y., Siewers, V., & Nielsen, J. (2020) · Nature Catalysis · doi:10.1038/s41929-019-0409-1 · Cited by 147 · see citing works
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O’Connell, J. D., Zhao, A. S., Ellington, A. D., & Marcotte, E. M. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155841 · Cited by 135 · see citing works
Greseth, M. D., & Traktman, P. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004021 · Cited by 125 · see citing works
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Rudolph, M. C., Monks, J., Burns, V., Phistry, M. M., Marians, R. C., Foote, M. R., Bauman, D. E., Anderson, S. M., & Neville, M. C. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00376.2010 · Cited by 117 · see citing works
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Polyak, S. W., Abell, A. D., Wilce, M. C. J., Zhang, L., & Booker, G. W. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3796-z · Cited by 93 · see citing works
Resnyk, C., Carré, W., Wang, X., Porter, T. E., Simon, J., Bihan-Duval, É. L., Duclos, M. J. M. J., Aggrey, S. E., & Cogburn, L. A. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-557 · Cited by 90 · see citing works
Moon, Y.-A., Ochoa, C. R., Mitsche, M. A., Hammer, R. E., & Horton, J. D. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m054353 · Cited by 83 · see citing works
Self-citationMetabolic regulation via enzyme filamentation
Aughey, G., & Liu, J. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2016.1172555 · Cited by 80 · see citing works
Crystal structure of Spot 14, a modulator of fatty acid synthesis
Colbert, C. L., Kim, C.-W., Moon, Y.-A., Henry, L., Palnitkar, M., McKean, W. B., Fitzgerald, K. J., Deisenhofer, J., Horton, J. D., & Kwon, H. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012736107 · Cited by 70 · see citing works
Self-citationMilk fat components with potential anticancer activity—a review
Rodríguez-Alcalá, L. M., Castro-Gómez, M. P., Pimentel, L. L., & Fontecha, J. (2017) · Bioscience Reports · doi:10.1042/bsr20170705 · Cited by 68 · see citing works
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Neelagandan, N., Gonnella, G., Dang, S., Janiesch, P. C., Miller, K. K., Küchler, K., Marques, R. F., Indenbirken, D., Alawi, M., Grundhoff, A. T., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky972 · Cited by 67 · see citing works
Moisá, S. J., Shike, D. W. W., Faulkner, D. B., Meteer, W. T., Keisler, D. H., & Loor, J. J. (2014) · Gene Regulation and Systems Biology · doi:10.4137/grsb.s11782 · Cited by 61 · see citing works
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Li, X.-J., Mu, Y., Li, T., Yang, Y., Zhang, M.-T., Li, Y.-S., Zhang, W. K., Tang, H., & Shang, H. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b03504 · Cited by 46 · see citing works
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Wang, X., Dou, X., Wu, J., & Meng, F. (2021) · Environmental Research · doi:10.1016/j.envres.2021.110873 · Cited by 42 · see citing works
Rudolph, M. C., Wellberg, E. A., Lewis, A. S., Terrell, K. L., Merz, A. L., Maluf, N. K., Serkova, N. J., & Anderson, S. M. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m044487 · Cited by 41 · see citing works
Yao, D., Luo, J., He, Q., Wu, M., Shi, H., Wang, H., Wang, M., Xu, H., & Loor, J. J. (2016) · Journal of Dairy Science · doi:10.3168/jds.2015-10632 · Cited by 38 · see citing works
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Park, S., Hwang, I., Makishima, Y., Perales‐Clemente, E., Kato, T., Niederländer, N. J., Park, E. Y., & Terzic, A. (2013) · Journal of Molecular Recognition · doi:10.1002/jmr.2313 · Cited by 25 · see citing works
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Shen, L., Luo, J., Du, J., Liu, C., Wu, X., Pu, Q., Fu, Y., Tang, Q., Liu, Y., Li, Q., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135978 · Cited by 23 · see citing works
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Polley, S., Lyumkis, D., & Horton, N. C. (2019) · Structure · doi:10.1016/j.str.2019.08.001 · Cited by 23 · see citing works
17β-Estradiol Modulates Gene Expression in the Female Mouse Cerebral Cortex
Humphreys, G. I., Ziegler, Y., & Nardulli, A. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111975 · Cited by 22 · see citing works
Pei, Y., Yue, L., Zhang, W., Wang, Y., Wen, B., Zhong, L., Xiang, J., Li, J., Zhang, S., Wang, H., et al. (2015) · Scientific Reports · doi:10.1038/srep16539 · Cited by 21 · see citing works
Wang, L., Xue, K., Wang, Y., Niu, L., Li, L., Zhong, T., Guo, J., Feng, J., Song, T., & Zhang, H. (2018) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.17.0407 · Cited by 21 · see citing works
Chaturvedi, S., Gupta, A. K., Bhattacharya, A., Dutta, T., Nain, L., & Khare, S. K. (2020) · Journal of Basic Microbiology · doi:10.1002/jobm.202000407 · Cited by 20 · see citing works
Sugiyama, M., TAKENAGA, F., Kitani, Y., Yamamoto, G., Okamoto, H., Masaoka, T., Araki, K., Nagoya, H., & Mori, T. (2012) · Biology Open · doi:10.1242/bio.20121263 · Cited by 21 · see citing works
Agglomeration: when folded proteins clump together
Romero, M. L. R., & Garcia‐Seisdedos, H. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01172-4 · Cited by 18 · see citing works
Milk lipid regulation at the maternal-offspring interface
Yang, D., Huynh, H., & Wan, Y. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.10.012 · Cited by 19 · see citing works
Tomar, M. S., Kumar, A., & Shrivastava, A. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.149382 · Cited by 19 · see citing works
Yang, X., Zhang, W., & Zhu, W. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e14896 · Cited by 16 · see citing works
Acetyl CoA carboxylase inactivation and meiotic maturation in mouse oocytes
Valsangkar, D., & Downs, S. M. (2015) · Molecular Reproduction and Development · doi:10.1002/mrd.22505 · Cited by 16 · see citing works
Chiu, Y., Husain, A., Sze, K. M., Ho, D. W., Suarez, E. M. S., Wang, X., Lee, E., Ma, H., Lee, J. M., Chan, L., et al. (2023) · Hepatology · doi:10.1097/hep.0000000000000266 · Cited by 15 · see citing works
A fast-acting lipid checkpoint in G1 prevents mitotic defects
Köberlin, M. S., Fan, Y., Liu, C., Chung, M., Pinto, A. F. M., Jackson, P. K., Saghatelian, A., & Meyer, T. (2024) · Nature Communications · doi:10.1038/s41467-024-46696-9 · Cited by 15 · see citing works
Cohen, L. D., Ziv, T., & Ziv, N. E. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1038614 · Cited by 14 · see citing works
Probing the Run-On Oligomer of Activated SgrAI Bound to DNA
Shah, S., Sanchez, J. L., Stewart, A. M., Piperakis, M. M., Cosstick, R., Nichols, C., Park, C. K., Ma, X., Wysocki, V. H., Bitinaite, J., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124783 · Cited by 14 · see citing works
Cox, T. C. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5398-7_8 · Cited by 14 · see citing works
Shaw, I., O'Sullivan, E. D., Pisco, A. O., Borthwick, G., Gallagher, K., Péault, B., Hughes, J., & Ferenbach, D. A. (2021) · Stem Cells Translational Medicine · doi:10.1002/sctm.20-0392 · Cited by 12 · see citing works
Shashikadze, B., Valla, L., Lombardo, S. D., Prehn, C. P., Haid, M., Riols, F., Stöckl, J. B., Elkhateib, R., Renner, S., Rathkolb, B., et al. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101768 · Cited by 13 · see citing works
Chen, H., Qin, J., Zhu, Y.-J., Pan, Z.-T., Xie, Y.-N., Jiao, M.-H., Chen, G., Chen, H., & Chu, M. (2012) · Asian Journal of Animal and Veterinary Advances · doi:10.3923/ajava.2012.802.811 · Cited by 13 · see citing works
Hwang, I., Makishima, Y., Kato, T., Park, S., Terzic, A., & Park, E. Y. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5715-6 · Cited by 12 · see citing works
Self-citationPark, C. K., Sanchez, J. L., Barahona, C. J., Basantes, L. E., Sanchez, J. C., Hernandez, C., & Horton, N. C. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003682 · Cited by 11 · see citing works
Barahona, C. J., Basantes, L. E., Tompkins, K. J., Heitman, D. M., Chukwu, B. I., Sanchez, J. C., Sanchez, J. L., Ghadirian, N., Park, C. K., & Horton, N. C. (2018) · Journal of Virology · doi:10.1128/jvi.01647-18 · Cited by 11 · see citing works
Rymut, S. M., Lu, B., Perez, A., Corey, D. A., Lamb, K., Cotton, C. U., & Kelley, T. J. (2019) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00369.2018 · Cited by 10 · see citing works
Mao, N., Zhao, Y., Dai, D., Yao, C., Liu, H., Fang, L., Wang, B., Zhang, Y., & Cao, J. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22941 · Cited by 10 · see citing works
Park, C. K., Sanchez, J. L., Barahona, C. J., Basantes, L. E., Sanchez, J. C., Hernandez, C., & Horton, N. C. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003680 · Cited by 10 · see citing works
Wang, Y., Wang, X., Luo, Y., Zhang, J., Lin, Y., Wu, J. J., Zeng, B., Liu, L., Yan, P., Liang, J.-Y., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010746 · Cited by 8 · see citing works
El‐Darzi, N., Mast, N., Li, Y., & Pikuleva, I. A. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05056-4 · Cited by 9 · see citing works
Activity and structure of human acetyl‐CoA carboxylase targeted by a specific inhibitor
Jang, S., Górnicki, P., Marjanovic, J., Bass, E., Iurcotta, T., Rodriguez, P. J., Austin, J. R., & Haselkorn, R. (2018) · FEBS Letters · doi:10.1002/1873-3468.13097 · Cited by 9 · see citing works
Winter is coming: Regulation of cellular metabolism by enzyme polymerization in dormancy and disease
Montrose, K., Cabezas, R. M. L., Paukštytė, J., & Saarikangas, J. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112383 · Cited by 9 · see citing works
Mast, N., Butts, M., & Pikuleva, I. A. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100555 · Cited by 8 · see citing works
Lamichhane, G., Lee, D., Franks, R., Olawale, F., Jin, J.-B., Egan, J. M., & Kim, Y. (2024) · Biology · doi:10.3390/biology13070472 · Cited by 8 · see citing works
Fang, P., Ye, S., Luo, Z., Guo, R., Jiang, Y., Liu, L., Li, S., & Xiao, F. (2025) · Environmental Pollution · doi:10.1016/j.envpol.2025.126566 · Cited by 7 · see citing works
Izumi, A., Hiraguchi, H., Kodaka, M., Ikeuchi, E., Narita, J., Kobayashi, R., Matsumoto, Y., Suzuki, T., Yamamoto, Y., Sato, R., et al. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.06.040 · Cited by 7 · see citing works
Landgraf, A., Okada, J., Horton, M., Liu, L. P., Solomon, S., Qiu, Y., Kurland, I. J., Sidoli, S., Pessin, J. E., & Shinoda, K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.15.649020 · Cited by 7 · see citing works
Activation of hepatic acetyl-CoA carboxylase by S-nitrosylation in response to diet
Venetos, N. M., Stomberski, C. T., Qian, Z., Premont, R. T., & Stamler, J. S. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100542 · Cited by 6 · see citing works
Suh, J. Y., Lee, H., Sim, D. Y., Park, J. E., Ahn, C., Park, S., Shin, N., Kim, B., Shim, B. S., & Kim, S. (2022) · Phytotherapy Research · doi:10.1002/ptr.7584 · Cited by 6 · see citing works
Self-citationLin, Y., Wang, R., Li, F., Lu, Z., Luo, W., Lu, H., Xu, Z., Xu, C., Lu, Y., Zhu, Z., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2504904123 · Cited by 5 · see citing works
- Authors
- Kim, C.-W., Moon, Y.-A., Park, S. W., Cheng, D., Kwon, H. J., & Horton, J. D.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Bristol-Myers Squibb (United States) (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-05-08
- Volume
- 107
- Issue
- 21
- Pages
- 9626-9631
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2906888
- OpenAlex
- W2023893231
- Cited by
- 136
- References
- 31
- Citations by year
- 2026: 3 · 2025: 12 · 2024: 12 · 2023: 9 · 2022: 9 · 2021: 8 · 2020: 7 · 2019: 9 · 2018: 14 · 2017: 6 · 2016: 5 · 2015: 8 · 2014: 9 · 2013: 6 · 2012: 9
- FWCI
- 2.52
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- YUHSpace (Yonsei University Medical Library) (submittedVersion, cc-by)
- Funders
- National Institutes of Health (HL20948)
- National Heart, Lung, and Blood Institute (HL 38049, HL-20948, R01HL038049, P01HL020948)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- acetyl-CoA carboxylase, protein polymerization, fatty acid synthesis, citrate activation, enzyme regulation, triglyceride accumulation, hepatic steatosis, liver
- MeSH terms
- Acetyl-CoA Carboxylase, Animals, Cytosol, Fatty Acids, Male, Mice, Inbred C57BL, Microtubule-Associated Proteins, Phosphorylation, Protein Binding, Mice, Protein Multimerization
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