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Article: Direct interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoter
Title | Direct interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoter |
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Authors | |
Issue Date | 2007 |
Publisher | American 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? |
Abstract | To 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 Identifier | http://hdl.handle.net/10722/183379 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Griffin, MJ | en_US |
dc.contributor.author | Wong, RHF | en_US |
dc.contributor.author | Pandya, N | en_US |
dc.contributor.author | Sul, HS | en_US |
dc.date.accessioned | 2013-05-27T07:11:38Z | - |
dc.date.available | 2013-05-27T07:11:38Z | - |
dc.date.issued | 2007 | en_US |
dc.identifier.citation | Journal Of Biological Chemistry, 2007, v. 282 n. 8, p. 5453-5467 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/183379 | - |
dc.description.abstract | To 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.language | eng | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Cell Line | en_US |
dc.subject.mesh | Drosophila | en_US |
dc.subject.mesh | Fatty Acid Synthetase Complex - Biosynthesis - Genetics | en_US |
dc.subject.mesh | Glycerol-3-Phosphate O-Acyltransferase - Biosynthesis - Genetics | en_US |
dc.subject.mesh | Insulin - Metabolism | en_US |
dc.subject.mesh | Mice | en_US |
dc.subject.mesh | Mitochondrial Proteins - Biosynthesis - Genetics | en_US |
dc.subject.mesh | Response Elements - Physiology | en_US |
dc.subject.mesh | Sterol Regulatory Element Binding Protein 1 - Agonists - Chemistry - Genetics - Metabolism | en_US |
dc.subject.mesh | Upstream Stimulatory Factors - Agonists - Chemistry - Genetics - Metabolism | en_US |
dc.title | Direct interaction between USF and SREBP-1c mediates synergistic activation of the fatty-acid synthase promoter | en_US |
dc.type | Article | en_US |
dc.identifier.email | Wong, RHF: rogerwg@hku.hk | en_US |
dc.identifier.authority | Wong, RHF=rp01754 | en_US |
dc.description.nature | link_to_OA_fulltext | en_US |
dc.identifier.doi | 10.1074/jbc.M610566200 | en_US |
dc.identifier.pmid | 17197698 | - |
dc.identifier.scopus | eid_2-s2.0-34247119238 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-34247119238&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 282 | en_US |
dc.identifier.issue | 8 | en_US |
dc.identifier.spage | 5453 | en_US |
dc.identifier.epage | 5467 | en_US |
dc.identifier.isi | WOS:000244482300040 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Griffin, MJ=42662896400 | en_US |
dc.identifier.scopusauthorid | Wong, RHF=16231857500 | en_US |
dc.identifier.scopusauthorid | Pandya, N=16231043200 | en_US |
dc.identifier.scopusauthorid | Sul, HS=55664145900 | en_US |
dc.identifier.issnl | 0021-9258 | - |