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ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation
Open accessAbstract
Chromatin Modifier Modulates Gene Expression: Modification of chromatin structure is usually thought of as a global, relatively nonspecific way of modulating gene expression. However, Wellen et al. (p. 1076 ; see the Perspective by Rathmell and Newgard ) demonstrate that such regulation helps link growth factor–stimulated increases in metabolism to appropriate changes in gene expression. Adenosine triphosphate (ATP)–citrate lyase (ACL), which converts citrate to acetyl–coenzyme A (CoA) in the mitochondria of mammalian cells during metabolism of glucose, was also found to be present in the nucleus, where it might regulate activity of histone acetyl transferases (HATs) by controlling the availability of acetyl-CoA. Indeed, depletion of ACL from cultured human colon carcinoma cells specifically decreased histone acetylation in the nucleus, but appeared not to affect the overall amount of acetylation of proteins in the cells. Loss of ACL in cultured mouse 3T3-L1 cells diminished the increase in histone acetylation normally associated with hormone-stimulated differentiation of these cells and inhibited the increase in expression of specific genes, such as that encoding the Glut4 glucose transporter. Thus, ACL may help cells link metabolic activity to changes in gene expression.
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In the citing paper
“the production of acetyl-CoA in HeLa cells necessary to drive histone acetylation has been attributed to the enzymatic conversion of citrate into oxaloacetate and acetyl-CoA via the ATP citrate lyase enzyme”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Wellen et al., 2009
In the citing paper
“the GCN5 histone acetyltransferase enzyme of the SAGA complex is of critical importance for histone acetylation in response to the combined provision of glucose and growth factors to otherwise quiescent cells.”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Wellen et al., 2009
In the citing paper
“cancer cells make acetyl-CoA via a fundamentally different pathway than prototrophic yeast”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Wellen et al., 2009
In the citing paper
“However, citrate export to the cytosol and subsequent cleavage by ACL provides a major source of cytosolic acetyl-CoA that is the obligate substrate for both de novo lipid synthesis and protein acetylation reactions (39, 187, 188).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [39]
In the citing paper
“Furthermore, studies have shown that both the glucose- and oncogene-driven increases in global histone acetylation are blocked by ACLY inhibition (Lee et al., 2014; Wellen et al., 2009).”
From The emerging hallmarks of cancer metabolism (2016) · cites this paper as Wellen et al., 2009
In the citing paper
“Acetylation requires a pool of the metabolite acetyl-CoA in the nucleus.155”
From Epigenetic mechanisms of major depression: Targeting neuronal plasticity (2018) · cites this paper as [155]
In the citing paper
“Glucose availability and acetyl-CoA production can also influence epigenetics by regulating the cytosolic acetyl-CoA pools available for histone acetylation reactions (51), raising the prospect that glucose-dependent metabolic flux may help drive or reinforce T cell differentiation programs.”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [51]
In the citing paper
“The acetyl-CoA groups used to modify histones are predominantly produced by acetyl-CoA synthetase in yeast and ATP-citrate lyase in mammalian cells, both of which enter the nucleus to produce a localized acetyl-CoA pool for this purpose (Figure 2).”
From Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us? (2012) · cites this paper as Wellen et al., 2009
In the citing paper
“Loss of function of these enzymes reduces histone acetylation, with global consequences on gene expression (Takahashi et al., 2006; Wellen et al., 2009).”
From Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us? (2012) · cites this paper as Wellen et al., 2009
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Metadata
- Authors
- Wellen, K. E., Hatzivassiliou, G., Sachdeva, U. M., Bui, T. V., Cross, J. R., & Thompson, C. B.
- Affiliations
- University of Pennsylvania (US)
- Venue
- Science
- Published
- 2009-05-22
- Volume
- 324
- Issue
- 5930
- Pages
- 1076-1080
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2746744
- OpenAlex
- W2144575277
- Cited by
- 2,298
- References
- 32
- Citations by year
- 2026: 194 · 2025: 158 · 2024: 150 · 2023: 169 · 2022: 167 · 2021: 185 · 2020: 149 · 2019: 163 · 2018: 131 · 2017: 122 · 2016: 111 · 2015: 131 · 2014: 118 · 2013: 87 · 2012: 96
- FWCI
- 35.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (T32-HL07439-27, T32HL007439)
- National Cancer Institute (R01CA092660, R01CA105463)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- ATP citrate lyase, histone acetylation, histone acetyltransferase, chromatin modification, gene expression regulation, cellular metabolism, glucose metabolism, 3T3-L1 adipocytes, adipogenesis, colon cancer cells, growth factor signaling
- MeSH terms
- Acetyl Coenzyme A, Acetate-CoA Ligase, Acetylation, Animals, ATP Citrate (pro-S)-Lyase, Cell Differentiation, Cell Line, Cell Nucleus, Cytoplasm, Gene Expression Regulation, Glucose, Glycolysis, Histone Deacetylases, Histones, Humans, Interleukin-3, Transcription, Genetic, 3T3 Cells, Adipocytes, Citric Acid, RNA Interference, Intercellular Signaling Peptides and Proteins, Cell Line, Tumor, Cell Proliferation, Mice, Histone Deacetylase Inhibitors
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