ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation

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 hist...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2009-05, Vol.324 (5930), p.1076-1080
Main Authors: Wellen, Kathryn E, Hatzivassiliou, Georgia, Sachdeva, Uma M, Bui, Thi V, Cross, Justin R, Thompson, Craig B
Format: Article
Language:English
Subjects:
3T3 Cells
Acetate-CoA Ligase - genetics
Acetate-CoA Ligase - metabolism
Acetates
Acetyl Coenzyme A - metabolism
Acetylation
Adipocytes
Adipocytes - cytology
Adipocytes - metabolism
Animals
ATP Citrate (pro-S)-Lyase - genetics
ATP Citrate (pro-S)-Lyase - metabolism
Biochemistry
Biological and medical sciences
Cell Differentiation
Cell Line
Cell Line, Tumor
Cell lines
Cell metabolism, cell oxidation
Cell Nucleus - enzymology
Cell physiology
Cell Proliferation
Cellular biology
Cellular differentiation
Cellular metabolism
Chromatin
Citric Acid - metabolism
Cytoplasm - enzymology
Enzymes
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
Glucose
Glucose - metabolism
Glycolysis
HCT116 cells
Histone Deacetylase Inhibitors
Histone Deacetylases - metabolism
Histones
Histones - metabolism
Humans
Intercellular Signaling Peptides and Proteins - metabolism
Interleukin-3 - metabolism
Metabolism
Metazoa
Mice
Molecular and cellular biology
RNA Interference
Small interfering RNA
Transcription, Genetic
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c653t-758fb2485269106ec8207cf7a71bae8929310b776115bd81d2a4c5af2124041c3
cites cdi_FETCH-LOGICAL-c653t-758fb2485269106ec8207cf7a71bae8929310b776115bd81d2a4c5af2124041c3
container_end_page 1080
container_issue 5930
container_start_page 1076
container_title Science (American Association for the Advancement of Science)
container_volume 324
creator Wellen, Kathryn E
Hatzivassiliou, Georgia
Sachdeva, Uma M
Bui, Thi V
Cross, Justin R
Thompson, Craig B
description 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.
doi_str_mv 10.1126/science.1164097
format article
fullrecord <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2746744</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>20494000</jstor_id><sourcerecordid>20494000</sourcerecordid><originalsourceid>FETCH-LOGICAL-c653t-758fb2485269106ec8207cf7a71bae8929310b776115bd81d2a4c5af2124041c3</originalsourceid><addsrcrecordid>eNqFks1v1DAQxS0EokvhzAmIkOAWOv6OL0jLitJKi0CiPVuO1ylesnGxk0r73zNooxZ66cUj6_38NDPPhLyk8IFSpk6Kj2HwAS9KgNGPyIKCkbVhwB-TBQBXdQNaHpFnpWwBUDP8KTmiRiiK6oJ8Wl58r1dxzG4M1XrvCp5x-FWqVej7qXe5-hpG16Y-ll01puosljENoVr6MO57N8Y0PCdPOteX8GKux-Ty9PPF6qxef_tyvlqua68kH2stm65lopFMGQoq-IaB9p12mrYuNIYZTqHVWlEq201DN8wJL13HKBMgqOfH5OPB93pqd2Hjw4Bd9_Y6x53Le5tctP8rQ_xpr9KNZVooLQQavJ8Ncvo9hTLaXSwe53RDSFOxSjMteSMfBLlippFUPQgyUIxKzhF8ew_cpikPuC7LKJem0WAQOjlAPqdScuhuZ6Ng_8Zt57jtHDe-eP3vSu74OV8E3s2AK971XXaDj-WWw-ZwDA3IvTpwW4w33-kgjMBvg_qbg965ZN1VRo_LHwwoB9wCEpL_AdPexOc</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>213598709</pqid></control><display><type>article</type><title>ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation</title><source>American Association for the Advancement of Science EJournals</source><source>Alma/SFX Local Collection</source><source>JSTOR</source><creator>Wellen, Kathryn E ; Hatzivassiliou, Georgia ; Sachdeva, Uma M ; Bui, Thi V ; Cross, Justin R ; Thompson, Craig B</creator><creatorcontrib>Wellen, Kathryn E ; Hatzivassiliou, Georgia ; Sachdeva, Uma M ; Bui, Thi V ; Cross, Justin R ; Thompson, Craig B</creatorcontrib><description>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.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1164097</identifier><identifier>PMID: 19461003</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>3T3 Cells ; Acetate-CoA Ligase - genetics ; Acetate-CoA Ligase - metabolism ; Acetates ; Acetyl Coenzyme A - metabolism ; Acetylation ; Adipocytes ; Adipocytes - cytology ; Adipocytes - metabolism ; Animals ; ATP Citrate (pro-S)-Lyase - genetics ; ATP Citrate (pro-S)-Lyase - metabolism ; Biochemistry ; Biological and medical sciences ; Cell Differentiation ; Cell Line ; Cell Line, Tumor ; Cell lines ; Cell metabolism, cell oxidation ; Cell Nucleus - enzymology ; Cell physiology ; Cell Proliferation ; Cellular biology ; Cellular differentiation ; Cellular metabolism ; Chromatin ; Citric Acid - metabolism ; Cytoplasm - enzymology ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation ; Glucose ; Glucose - metabolism ; Glycolysis ; HCT116 cells ; Histone Deacetylase Inhibitors ; Histone Deacetylases - metabolism ; Histones ; Histones - metabolism ; Humans ; Intercellular Signaling Peptides and Proteins - metabolism ; Interleukin-3 - metabolism ; Metabolism ; Metazoa ; Mice ; Molecular and cellular biology ; RNA Interference ; Small interfering RNA ; Transcription, Genetic</subject><ispartof>Science (American Association for the Advancement of Science), 2009-05, Vol.324 (5930), p.1076-1080</ispartof><rights>Copyright 2009 American Association for the Advancement of Science</rights><rights>2009 INIST-CNRS</rights><rights>Copyright © 2009, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c653t-758fb2485269106ec8207cf7a71bae8929310b776115bd81d2a4c5af2124041c3</citedby><cites>FETCH-LOGICAL-c653t-758fb2485269106ec8207cf7a71bae8929310b776115bd81d2a4c5af2124041c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20494000$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20494000$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,777,781,882,2871,2872,27905,27906,58219,58452</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=21551670$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19461003$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wellen, Kathryn E</creatorcontrib><creatorcontrib>Hatzivassiliou, Georgia</creatorcontrib><creatorcontrib>Sachdeva, Uma M</creatorcontrib><creatorcontrib>Bui, Thi V</creatorcontrib><creatorcontrib>Cross, Justin R</creatorcontrib><creatorcontrib>Thompson, Craig B</creatorcontrib><title>ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>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.</description><subject>3T3 Cells</subject><subject>Acetate-CoA Ligase - genetics</subject><subject>Acetate-CoA Ligase - metabolism</subject><subject>Acetates</subject><subject>Acetyl Coenzyme A - metabolism</subject><subject>Acetylation</subject><subject>Adipocytes</subject><subject>Adipocytes - cytology</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>ATP Citrate (pro-S)-Lyase - genetics</subject><subject>ATP Citrate (pro-S)-Lyase - metabolism</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Differentiation</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Cell lines</subject><subject>Cell metabolism, cell oxidation</subject><subject>Cell Nucleus - enzymology</subject><subject>Cell physiology</subject><subject>Cell Proliferation</subject><subject>Cellular biology</subject><subject>Cellular differentiation</subject><subject>Cellular metabolism</subject><subject>Chromatin</subject><subject>Citric Acid - metabolism</subject><subject>Cytoplasm - enzymology</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation</subject><subject>Glucose</subject><subject>Glucose - metabolism</subject><subject>Glycolysis</subject><subject>HCT116 cells</subject><subject>Histone Deacetylase Inhibitors</subject><subject>Histone Deacetylases - metabolism</subject><subject>Histones</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Intercellular Signaling Peptides and Proteins - metabolism</subject><subject>Interleukin-3 - metabolism</subject><subject>Metabolism</subject><subject>Metazoa</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>RNA Interference</subject><subject>Small interfering RNA</subject><subject>Transcription, Genetic</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqFks1v1DAQxS0EokvhzAmIkOAWOv6OL0jLitJKi0CiPVuO1ylesnGxk0r73zNooxZ66cUj6_38NDPPhLyk8IFSpk6Kj2HwAS9KgNGPyIKCkbVhwB-TBQBXdQNaHpFnpWwBUDP8KTmiRiiK6oJ8Wl58r1dxzG4M1XrvCp5x-FWqVej7qXe5-hpG16Y-ll01puosljENoVr6MO57N8Y0PCdPOteX8GKux-Ty9PPF6qxef_tyvlqua68kH2stm65lopFMGQoq-IaB9p12mrYuNIYZTqHVWlEq201DN8wJL13HKBMgqOfH5OPB93pqd2Hjw4Bd9_Y6x53Le5tctP8rQ_xpr9KNZVooLQQavJ8Ncvo9hTLaXSwe53RDSFOxSjMteSMfBLlippFUPQgyUIxKzhF8ew_cpikPuC7LKJem0WAQOjlAPqdScuhuZ6Ng_8Zt57jtHDe-eP3vSu74OV8E3s2AK971XXaDj-WWw-ZwDA3IvTpwW4w33-kgjMBvg_qbg965ZN1VRo_LHwwoB9wCEpL_AdPexOc</recordid><startdate>20090522</startdate><enddate>20090522</enddate><creator>Wellen, Kathryn E</creator><creator>Hatzivassiliou, Georgia</creator><creator>Sachdeva, Uma M</creator><creator>Bui, Thi V</creator><creator>Cross, Justin R</creator><creator>Thompson, Craig B</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090522</creationdate><title>ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation</title><author>Wellen, Kathryn E ; Hatzivassiliou, Georgia ; Sachdeva, Uma M ; Bui, Thi V ; Cross, Justin R ; Thompson, Craig B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c653t-758fb2485269106ec8207cf7a71bae8929310b776115bd81d2a4c5af2124041c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>3T3 Cells</topic><topic>Acetate-CoA Ligase - genetics</topic><topic>Acetate-CoA Ligase - metabolism</topic><topic>Acetates</topic><topic>Acetyl Coenzyme A - metabolism</topic><topic>Acetylation</topic><topic>Adipocytes</topic><topic>Adipocytes - cytology</topic><topic>Adipocytes - metabolism</topic><topic>Animals</topic><topic>ATP Citrate (pro-S)-Lyase - genetics</topic><topic>ATP Citrate (pro-S)-Lyase - metabolism</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cell Differentiation</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>Cell lines</topic><topic>Cell metabolism, cell oxidation</topic><topic>Cell Nucleus - enzymology</topic><topic>Cell physiology</topic><topic>Cell Proliferation</topic><topic>Cellular biology</topic><topic>Cellular differentiation</topic><topic>Cellular metabolism</topic><topic>Chromatin</topic><topic>Citric Acid - metabolism</topic><topic>Cytoplasm - enzymology</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation</topic><topic>Glucose</topic><topic>Glucose - metabolism</topic><topic>Glycolysis</topic><topic>HCT116 cells</topic><topic>Histone Deacetylase Inhibitors</topic><topic>Histone Deacetylases - metabolism</topic><topic>Histones</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Intercellular Signaling Peptides and Proteins - metabolism</topic><topic>Interleukin-3 - metabolism</topic><topic>Metabolism</topic><topic>Metazoa</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>RNA Interference</topic><topic>Small interfering RNA</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wellen, Kathryn E</creatorcontrib><creatorcontrib>Hatzivassiliou, Georgia</creatorcontrib><creatorcontrib>Sachdeva, Uma M</creatorcontrib><creatorcontrib>Bui, Thi V</creatorcontrib><creatorcontrib>Cross, Justin R</creatorcontrib><creatorcontrib>Thompson, Craig B</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics &amp; Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical &amp; Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology &amp; Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts – Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wellen, Kathryn E</au><au>Hatzivassiliou, Georgia</au><au>Sachdeva, Uma M</au><au>Bui, Thi V</au><au>Cross, Justin R</au><au>Thompson, Craig B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2009-05-22</date><risdate>2009</risdate><volume>324</volume><issue>5930</issue><spage>1076</spage><epage>1080</epage><pages>1076-1080</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><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.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>19461003</pmid><doi>10.1126/science.1164097</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0036-8075
ispartof Science (American Association for the Advancement of Science), 2009-05, Vol.324 (5930), p.1076-1080
issn 0036-8075
1095-9203
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2746744
source American Association for the Advancement of Science EJournals; Alma/SFX Local Collection; JSTOR
subjects 3T3 Cells
Acetate-CoA Ligase - genetics
Acetate-CoA Ligase - metabolism
Acetates
Acetyl Coenzyme A - metabolism
Acetylation
Adipocytes
Adipocytes - cytology
Adipocytes - metabolism
Animals
ATP Citrate (pro-S)-Lyase - genetics
ATP Citrate (pro-S)-Lyase - metabolism
Biochemistry
Biological and medical sciences
Cell Differentiation
Cell Line
Cell Line, Tumor
Cell lines
Cell metabolism, cell oxidation
Cell Nucleus - enzymology
Cell physiology
Cell Proliferation
Cellular biology
Cellular differentiation
Cellular metabolism
Chromatin
Citric Acid - metabolism
Cytoplasm - enzymology
Enzymes
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
Glucose
Glucose - metabolism
Glycolysis
HCT116 cells
Histone Deacetylase Inhibitors
Histone Deacetylases - metabolism
Histones
Histones - metabolism
Humans
Intercellular Signaling Peptides and Proteins - metabolism
Interleukin-3 - metabolism
Metabolism
Metazoa
Mice
Molecular and cellular biology
RNA Interference
Small interfering RNA
Transcription, Genetic
title ATP-Citrate Lyase Links Cellular Metabolism to Histone Acetylation
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T14%3A45%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=ATP-Citrate%20Lyase%20Links%20Cellular%20Metabolism%20to%20Histone%20Acetylation&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Wellen,%20Kathryn%20E&rft.date=2009-05-22&rft.volume=324&rft.issue=5930&rft.spage=1076&rft.epage=1080&rft.pages=1076-1080&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.1164097&rft_dat=%3Cjstor_pubme%3E20494000%3C/jstor_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c653t-758fb2485269106ec8207cf7a71bae8929310b776115bd81d2a4c5af2124041c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=213598709&rft_id=info:pmid/19461003&rft_jstor_id=20494000&rfr_iscdi=true