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Article: Post-activation turn-off of NF-κB-dependent transcription is regulated by acetylation of p65

TitlePost-activation turn-off of NF-κB-dependent transcription is regulated by acetylation of p65
Authors
Issue Date2003
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, 2003, v. 278 n. 4, p. 2758-2766 How to Cite?
AbstractNF-κB represents a family of eukaryotic transcription factors participating in the regulation of various cellular genes involved in the immediate early processes of immune, acute-phase, and inflammatory responses. Cellular localization and consequently the transcriptional activity of NF-κB is tightly regulated by its partner IκBα. Here, we show that the p65 subunit of NF-κB is acetylated by both p300 and PCAF on lysines 122 and 123. Both HDAC2 and HDAC3 interact with p65, although only HDAC3 was able to deacetylate p65. Acetylation of p65 reduces its ability to bind κB-DNA. Finally, acetylation of p65 facilitated its removal from DNA and consequently its IκBα-mediated export from the nucleus. We propose that acetylation of p65 plays a key role in IκBα-mediated attenuation of NF-κB transcriptional activity which is an important process that restores the latent state in post-induced cells.
Persistent Identifierhttp://hdl.handle.net/10722/147481
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKiernan, Ren_US
dc.contributor.authorBrès, Ven_US
dc.contributor.authorNg, RWMen_US
dc.contributor.authorCoudart, MPen_US
dc.contributor.authorEl Messaoudi, Sen_US
dc.contributor.authorSardet, Cen_US
dc.contributor.authorJin, DYen_US
dc.contributor.authorEmiliani, Sen_US
dc.contributor.authorBenkirane, Men_US
dc.date.accessioned2012-05-29T06:04:01Z-
dc.date.available2012-05-29T06:04:01Z-
dc.date.issued2003en_US
dc.identifier.citationJournal of Biological Chemistry, 2003, v. 278 n. 4, p. 2758-2766en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147481-
dc.description.abstractNF-κB represents a family of eukaryotic transcription factors participating in the regulation of various cellular genes involved in the immediate early processes of immune, acute-phase, and inflammatory responses. Cellular localization and consequently the transcriptional activity of NF-κB is tightly regulated by its partner IκBα. Here, we show that the p65 subunit of NF-κB is acetylated by both p300 and PCAF on lysines 122 and 123. Both HDAC2 and HDAC3 interact with p65, although only HDAC3 was able to deacetylate p65. Acetylation of p65 reduces its ability to bind κB-DNA. Finally, acetylation of p65 facilitated its removal from DNA and consequently its IκBα-mediated export from the nucleus. We propose that acetylation of p65 plays a key role in IκBα-mediated attenuation of NF-κB transcriptional activity which is an important process that restores the latent state in post-induced cells.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.meshAcetylationen_US
dc.subject.meshAcetyltransferases - Metabolismen_US
dc.subject.meshCell Nucleus - Metabolismen_US
dc.subject.meshChromatin - Metabolismen_US
dc.subject.meshDna - Metabolismen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshGene Expression Regulation, Enzymologicen_US
dc.subject.meshHela Cellsen_US
dc.subject.meshHistone Acetyltransferasesen_US
dc.subject.meshHistone Deacetylase 2en_US
dc.subject.meshHistone Deacetylases - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshJurkat Cellsen_US
dc.subject.meshLysine - Metabolismen_US
dc.subject.meshModels, Biologicalen_US
dc.subject.meshNf-Kappa B - Metabolismen_US
dc.subject.meshNuclear Proteins - Metabolismen_US
dc.subject.meshPlasmids - Metabolismen_US
dc.subject.meshPrecipitin Testsen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Transporten_US
dc.subject.meshRepressor Proteins - Metabolismen_US
dc.subject.meshSaccharomyces Cerevisiae Proteins - Metabolismen_US
dc.subject.meshTrans-Activators - Metabolismen_US
dc.subject.meshTranscription Factor Relaen_US
dc.subject.meshTranscription, Geneticen_US
dc.titlePost-activation turn-off of NF-κB-dependent transcription is regulated by acetylation of p65en_US
dc.typeArticleen_US
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_US
dc.identifier.authorityJin, DY=rp00452en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1074/jbc.M209572200en_US
dc.identifier.pmid12419806-
dc.identifier.scopuseid_2-s2.0-0037462725en_US
dc.identifier.hkuros80473-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037462725&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume278en_US
dc.identifier.issue4en_US
dc.identifier.spage2758en_US
dc.identifier.epage2766en_US
dc.identifier.isiWOS:000180562000089-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridKiernan, R=6603797907en_US
dc.identifier.scopusauthoridBrès, V=6508307483en_US
dc.identifier.scopusauthoridNg, RWM=7102153861en_US
dc.identifier.scopusauthoridCoudart, MP=6507069815en_US
dc.identifier.scopusauthoridEl Messaoudi, S=6506335304en_US
dc.identifier.scopusauthoridSardet, C=7005616535en_US
dc.identifier.scopusauthoridJin, DY=7201973614en_US
dc.identifier.scopusauthoridEmiliani, S=7004242251en_US
dc.identifier.scopusauthoridBenkirane, M=7004581121en_US

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