What question did this study set out to answer?

Investigate the metabolic mechanism and enzymatic pathway responsible for supplying acetyl-CoA for histone acetylation and gene regulation in mammalian cells.

May 21, 2009ScienceOpen Access

ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation

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Authors

KWKathryn E. WellenCancer Research Institute GHGeorgia HatzivassiliouCancer Research Institute USUma M. SachdevaHarvard University

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Implication

Laboratory study demonstrates that ATP-citrate lyase drives histone acetylation from glucose in mammalian cells, indicating a direct link between nutrient metabolism and gene regulation.

Key Points

Investigate the metabolic mechanism and enzymatic pathway responsible for supplying acetyl-CoA for histone acetylation and gene regulation in mammalian cells.
Assessed histone acetylation levels in mammalian cell models across varying levels of glucose availability.
Evaluated the requirement of adenosine triphosphate (ATP)-citrate lyase (ACL) during growth factor stimulation and cellular differentiation.
Histone acetylation in mammalian cells depends on ATP-citrate lyase (ACL) to convert glucose-derived citrate into acetyl-CoA.
ACL activity is required for histone acetylation increases during growth factor signaling, differentiation, and glucose availability fluctuations, functionally linking nutrient metabolism to gene expression.

Cite This Study

Wellen et al. (2009) studied this question.

synapsesocial.com/papers/69b31e4c52eef3fac5b3f56b https://doi.org/10.1126/science.1164097

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Implication

Laboratory study demonstrates that ATP-citrate lyase drives histone acetylation from glucose in mammalian cells, indicating a direct link between nutrient metabolism and gene regulation.

ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation

Discussion

Member takes

Implication

Key Points

Cite This Study

ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation

Discussion

Member takes

Implication

Key Points

Cite This Study

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