Journal
SCIENCE
Volume 324, Issue 5930, Pages 1076-1080Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1164097
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Funding
- NIH [T32-HL07439-27]
- National Cancer Institute
- Damon Runyon Cancer Research Foundation [DRG-1955-07]
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Histone acetylation in single-cell eukaryotes relies on acetyl coenzyme A (acetyl-CoA) synthetase enzymes that use acetate to produce acetyl-CoA. Metazoans, however, use glucose as their main carbon source and have exposure only to low concentrations of extracellular acetate. We have shown that histone acetylation in mammalian cells is dependent on adenosine triphosphate (ATP)-citrate lyase (ACL), the enzyme that converts glucose-derived citrate into acetyl-CoA. We found that ACL is required for increases in histone acetylation in response to growth factor stimulation and during differentiation, and that glucose availability can affect histone acetylation in an ACL-dependent manner. Together, these findings suggest that ACL activity is required to link growth factor-induced increases in nutrient metabolism to the regulation of histone acetylation and gene expression.
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