ATP-citrate lyase controls a glucose-to-acetate metabolic switch
Open accessAbstract
Mechanisms of metabolic flexibility enable cells to survive under stressful conditions and can thwart therapeutic responses. Acetyl-coenzyme A (CoA) plays central roles in energy production, lipid metabolism, and epigenomic modifications. Here, we show that, upon genetic deletion of Acly, the gene coding for ATP-citrate lyase (ACLY), cells remain viable and proliferate, although at an impaired rate. In the absence of ACLY, cells upregulate ACSS2 and utilize exogenous acetate to provide acetyl-CoA for de novo lipogenesis (DNL) and histone acetylation. A physiological level of acetate is sufficient for cell viability and abundant acetyl-CoA production, although histone acetylation levels remain low in ACLY-deficient cells unless supplemented with high levels of acetate. ACLY-deficient adipocytes accumulate lipid in vivo, exhibit increased acetyl-CoA and malonyl-CoA production from acetate, and display some differences in fatty acid content and synthesis. Together, these data indicate that engagement of acetate metabolism is a crucial, although partial, mechanism of compensation for ACLY deficiency.
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- Authors
- Zhao, S., Torres, A., Henry, R. A., Trefely, S., Wallace, M., Lee, J. V., Carrer, A., Sengupta, A., Campbell, S. L., Kuo, Y.-M., Frey, A. J., Meurs, N., Viola, J. M., Blair, I. A., Weljie, A. M., Metallo, C. M., Snyder, N. W., Andrews, A. J., & Wellen, K. E.
- Affiliations
- University of Pennsylvania (US)
- Fox Chase Cancer Center (US)
- Drexel University (US)
- University of California San Diego (US)
- Corresponding author
- Wellen, Kathryn E.
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2016-10
- Volume
- 17
- Issue
- 4
- Pages
- 1037-1052
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC5175409
- OpenAlex
- W2536126966
- Cited by
- 394
- References
- 52
- Citations by year
- 2026: 34 · 2025: 44 · 2024: 46 · 2023: 52 · 2022: 44 · 2021: 44 · 2020: 37 · 2019: 37 · 2018: 38 · 2017: 15 · 2016: 2
- FWCI
- 12.77
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by-nc-nd)
- Funders
- American Diabetes Association
- University of Pennsylvania
- Abramson Cancer Center
- National Institutes of Health
- National Cancer Institute (T32CA115299, R01CA174761, F31CA189744, R01CA188652, P30CA006927, P30CA016520)
- National Institute of General Medical Sciences (R01GM102503, K12GM081259)
- National Institute of Environmental Health Sciences (K22ES026235, P30ES013508)
- Abramson Family Cancer Research Institute
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R21HD087866)
- 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 › Metabolism, Diabetes, and Cancer
- Keywords
- ATP citrate lyase, acetate metabolism, acetyl-CoA, de novo lipogenesis, histone acetylation, ACSS2, metabolic flexibility, adipocytes, lipid accumulation, malonyl-CoA, fatty acid synthesis, metabolic compensation
- MeSH terms
- Acetates, Acetyl Coenzyme A, Acetate-CoA Ligase, Acetylation, Animals, ATP Citrate (pro-S)-Lyase, Cell Survival, Fibroblasts, Glucose, Histones, Lipids, Male, Up-Regulation, Gene Deletion, Adipocytes, Cell Proliferation, Lipid Metabolism, Mice
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