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Article: Direct interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoter

TitleDirect interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoter
Authors
Issue Date2007
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2007, v. 282 n. 8, p. 5453-5467 How to Cite?
AbstractTo underst and the molecular mechanisms underlying transcriptional activation of fatty-acid synthase (FAS), we examined the relationship between upstream stimulatory factor (USF) and SREBP-1c, two transcription factors that we have shown previously to be critical for FAS induction by feeding/insulin. Here, by using a combination of tandem affinity purification and coimmunoprecipitation, we demonstrate, for the first time, that USF and SREBP-1 interact in vitro and in vivo. Glutathione S-transferase pulldown experiments with various USF and sterol regulatory element-binding protein (SREBP) deletion constructs indicate that the basic helix-loop-helixdomain of USF interacts directly with the basic helix-loop-helix and an N-terminal region of SREBP-1c. Furthermore, cotransfection of USF and SREBP-1c with an FAS promoter-luciferase reporter construct in Drosophila SL2 cells results in highly synergistic activation of the FAS promoter. We also show similar cooperative activation of the mitochondrial glycerol-3-phosphate acyltransferase promoter by USF and SREBP-1c. Chromatin immunoprecipitation analysis of mouse liver demonstrates that USF binds constitutively to the mitochondrial glycerol 3-phosphate acyltransferase promoter during fasting/refeeding in vivo, whereas binding of SREBP-1 is observed only during refeeding, in a manner identical to that of the FAS promoter. In addition, we show that the synergy we have observed depends on the activation domains of both proteins and that mutated USF or SREBP lacking the N-terminal activation domain could inhibit the transactivation of the other. Closely positioned E-boxes and sterol regulatory elements found in the promoters of several lipogenic genes suggest a common mechanism of induction by feeding/insulin. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/183379
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGriffin, MJen_US
dc.contributor.authorWong, RHFen_US
dc.contributor.authorPandya, Nen_US
dc.contributor.authorSul, HSen_US
dc.date.accessioned2013-05-27T07:11:38Z-
dc.date.available2013-05-27T07:11:38Z-
dc.date.issued2007en_US
dc.identifier.citationJournal Of Biological Chemistry, 2007, v. 282 n. 8, p. 5453-5467en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/183379-
dc.description.abstractTo underst and the molecular mechanisms underlying transcriptional activation of fatty-acid synthase (FAS), we examined the relationship between upstream stimulatory factor (USF) and SREBP-1c, two transcription factors that we have shown previously to be critical for FAS induction by feeding/insulin. Here, by using a combination of tandem affinity purification and coimmunoprecipitation, we demonstrate, for the first time, that USF and SREBP-1 interact in vitro and in vivo. Glutathione S-transferase pulldown experiments with various USF and sterol regulatory element-binding protein (SREBP) deletion constructs indicate that the basic helix-loop-helixdomain of USF interacts directly with the basic helix-loop-helix and an N-terminal region of SREBP-1c. Furthermore, cotransfection of USF and SREBP-1c with an FAS promoter-luciferase reporter construct in Drosophila SL2 cells results in highly synergistic activation of the FAS promoter. We also show similar cooperative activation of the mitochondrial glycerol-3-phosphate acyltransferase promoter by USF and SREBP-1c. Chromatin immunoprecipitation analysis of mouse liver demonstrates that USF binds constitutively to the mitochondrial glycerol 3-phosphate acyltransferase promoter during fasting/refeeding in vivo, whereas binding of SREBP-1 is observed only during refeeding, in a manner identical to that of the FAS promoter. In addition, we show that the synergy we have observed depends on the activation domains of both proteins and that mutated USF or SREBP lacking the N-terminal activation domain could inhibit the transactivation of the other. Closely positioned E-boxes and sterol regulatory elements found in the promoters of several lipogenic genes suggest a common mechanism of induction by feeding/insulin. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Lineen_US
dc.subject.meshDrosophilaen_US
dc.subject.meshFatty Acid Synthetase Complex - Biosynthesis - Geneticsen_US
dc.subject.meshGlycerol-3-Phosphate O-Acyltransferase - Biosynthesis - Geneticsen_US
dc.subject.meshInsulin - Metabolismen_US
dc.subject.meshMiceen_US
dc.subject.meshMitochondrial Proteins - Biosynthesis - Geneticsen_US
dc.subject.meshResponse Elements - Physiologyen_US
dc.subject.meshSterol Regulatory Element Binding Protein 1 - Agonists - Chemistry - Genetics - Metabolismen_US
dc.subject.meshUpstream Stimulatory Factors - Agonists - Chemistry - Genetics - Metabolismen_US
dc.titleDirect interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoteren_US
dc.typeArticleen_US
dc.identifier.emailWong, RHF: rogerwg@hku.hken_US
dc.identifier.authorityWong, RHF=rp01754en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1074/jbc.M610566200en_US
dc.identifier.pmid17197698-
dc.identifier.scopuseid_2-s2.0-34247119238en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34247119238&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume282en_US
dc.identifier.issue8en_US
dc.identifier.spage5453en_US
dc.identifier.epage5467en_US
dc.identifier.isiWOS:000244482300040-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridGriffin, MJ=42662896400en_US
dc.identifier.scopusauthoridWong, RHF=16231857500en_US
dc.identifier.scopusauthoridPandya, N=16231043200en_US
dc.identifier.scopusauthoridSul, HS=55664145900en_US

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