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Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12 provides a tertiary level of regulation of fatty acid synthesis
Open accessAbstract
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.83”
From The multifaceted contributions of mitochondria to cellular metabolism (2018) · cites this paper as [83]
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Metadata
- 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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