Cited by 137Cancer, Lipids, and MetabolismLipid metabolism and biosynthesisPeroxisome Proliferator-Activated Receptors

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Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12 provides a tertiary level of regulation of fatty acid synthesis

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Kim, Chai-Wan, Moon, Young-Ah, Park, Sahng Wook, Cheng, Dong, Kwon, Hyock Joo, Horton, Jay D.·2010·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1001292107PMC PMC2906888

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Abstract

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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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)
ORCID: Kim, Chai-Wan
Moon, Young-Ah
Park, Sahng Wook
Cheng, Dong
Horton, Jay D.
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
DOI: 10.1073/pnas.1001292107
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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Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12 provides a tertiary level of regulation of fatty acid synthesis

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