ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation Export

@article{citeulike:4634222, abstract = {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. 10.1126/science.1164097}, author = {Wellen, Kathryn E. and Hatzivassiliou, Georgia and Sachdeva, Uma M. and Bui, Thi V. and Cross, Justin R. and Thompson, Craig B.}, citeulike-article-id = {4634222}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1164097}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/324/5930/1076?sa_campaign=Email}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19461003}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19461003}, day = {22}, doi = {10.1126/science.1164097}, journal = {Science}, keywords = {acetylation, glucose, histone-modification, metabolism}, month = {May}, number = {5930}, pages = {1076--1080}, posted-at = {2009-05-28 21:59:47}, priority = {2}, title = {ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation}, url = {http://dx.doi.org/10.1126/science.1164097}, volume = {324}, year = {2009} }

TY - JOUR ID - citeulike:4634222 L3 - citeulike-article-id:4634222 N2 - 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. 10.1126/science.1164097 IS - 5930 JF - Science EP - 1080 TI - ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation VL - 324 SP - 1076 KW - acetylation KW - glucose KW - histone-modification KW - metabolism AU - Wellen, Kathryn AU - Hatzivassiliou, Georgia AU - Sachdeva, Uma AU - Bui, Thi AU - Cross, Justin AU - Thompson, Craig PY - 2009/05/22/ UR - http://dx.doi.org/10.1126/science.1164097 ER -