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Article: Interactions with p300 enhance transcriptional activation by the PDZ-domain coactivator Bridge-1

TitleInteractions with p300 enhance transcriptional activation by the PDZ-domain coactivator Bridge-1
Authors
Issue Date2005
PublisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.org
Citation
Journal Of Endocrinology, 2005, v. 187 n. 2, p. 283-292 How to Cite?
Abstract
Transcriptional coactivators are essential mediators of signal amplification in the regulation of gene expression in response to hormones and extracellular signals. We previously identified Bridge-1 (PSMD9) as a PDZ-domain coregulator that augments insulin gene transcription via interactions with the basic helix-loop-helix transcription factors E12 and E47, and that increases transcriptional activation by the homeodomain transcription factor PDX-1. In these studies, we find that transcriptional activation by Bridge-1 can be regulated via interactions with the histone acetyltransferase and nuclear receptor coactivator p300. In transfection assays, transcriptional activation by Bridge-1 is increased by the inhibition of endogenous histone deacetylase activity with trichostatin A, indicating that the transcriptional activation function of Bridge-1 can be regulated by histone modifications. The exogenous expression of p300 enhances the transcriptional activation by Bridge-1 in a dose-dependent manner. In contrast, the sequestration of p300 by the overexpression of the adenoviral protein E1A, but not by an E1A mutant protein that is unable to interact with p300, suppresses the transcriptional activation by Bridge-1. We demonstrate that p300 and Bridge-1 proteins interact in immunoprecipitation and glutathione-S-transferase (GST) pull-down assays. Bridge-1 interacts directly with multiple regions within p300 that encompass C/H1 or C/H2 cysteine- and histidine-rich protein interaction domains and the histone acetyltransferase domain. Deletion or point mutagenesis of the Bridge-1 PDZ domain substantially reduces transcriptional activation by Bridge-1 and interrupts interactions with p300. We propose that p300 interactions with Bridge-1 can augment the transcriptional activation of regulatory target genes by Bridge-1. © 2005 Society for Endocrinology.
Persistent Identifierhttp://hdl.handle.net/10722/68286
ISSN
2013 Impact Factor: 3.586
2013 SCImago Journal Rankings: 1.736
ISI Accession Number ID
References

 

Author Affiliations
  1. Massachusetts General Hospital
  2. The University of Hong Kong
DC FieldValueLanguage
dc.contributor.authorLee, JHen_HK
dc.contributor.authorVolinic, JLen_HK
dc.contributor.authorBanz, Cen_HK
dc.contributor.authorYao, KMen_HK
dc.contributor.authorThomas, MKen_HK
dc.date.accessioned2010-09-06T06:03:08Z-
dc.date.available2010-09-06T06:03:08Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of Endocrinology, 2005, v. 187 n. 2, p. 283-292en_HK
dc.identifier.issn0022-0795en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68286-
dc.description.abstractTranscriptional coactivators are essential mediators of signal amplification in the regulation of gene expression in response to hormones and extracellular signals. We previously identified Bridge-1 (PSMD9) as a PDZ-domain coregulator that augments insulin gene transcription via interactions with the basic helix-loop-helix transcription factors E12 and E47, and that increases transcriptional activation by the homeodomain transcription factor PDX-1. In these studies, we find that transcriptional activation by Bridge-1 can be regulated via interactions with the histone acetyltransferase and nuclear receptor coactivator p300. In transfection assays, transcriptional activation by Bridge-1 is increased by the inhibition of endogenous histone deacetylase activity with trichostatin A, indicating that the transcriptional activation function of Bridge-1 can be regulated by histone modifications. The exogenous expression of p300 enhances the transcriptional activation by Bridge-1 in a dose-dependent manner. In contrast, the sequestration of p300 by the overexpression of the adenoviral protein E1A, but not by an E1A mutant protein that is unable to interact with p300, suppresses the transcriptional activation by Bridge-1. We demonstrate that p300 and Bridge-1 proteins interact in immunoprecipitation and glutathione-S-transferase (GST) pull-down assays. Bridge-1 interacts directly with multiple regions within p300 that encompass C/H1 or C/H2 cysteine- and histidine-rich protein interaction domains and the histone acetyltransferase domain. Deletion or point mutagenesis of the Bridge-1 PDZ domain substantially reduces transcriptional activation by Bridge-1 and interrupts interactions with p300. We propose that p300 interactions with Bridge-1 can augment the transcriptional activation of regulatory target genes by Bridge-1. © 2005 Society for Endocrinology.en_HK
dc.languageengen_HK
dc.publisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.orgen_HK
dc.relation.ispartofJournal of Endocrinologyen_HK
dc.rightsJournal of Endocrinology. Copyright © Society for Endocrinology.en_HK
dc.subject.meshAdenovirus E1A Proteins - pharmacologyen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshBlotting, Westernen_HK
dc.subject.meshCells, Cultureden_HK
dc.subject.meshDiabetes Mellitus, Type 1 - metabolismen_HK
dc.subject.meshDose-Response Relationship, Drugen_HK
dc.subject.meshGene Deletionen_HK
dc.subject.meshGlutathione Transferase - metabolismen_HK
dc.subject.meshHelix-Loop-Helix Motifsen_HK
dc.subject.meshHistone Deacetylase Inhibitorsen_HK
dc.subject.meshHydroxamic Acids - pharmacologyen_HK
dc.subject.meshImmunoprecipitationen_HK
dc.subject.meshInsulin - metabolismen_HK
dc.subject.meshMutagenesis, Site-Directeden_HK
dc.subject.meshPoint Mutationen_HK
dc.subject.meshProteasome Endopeptidase Complexen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshProteins - genetics - metabolismen_HK
dc.subject.meshTranscription, Geneticen_HK
dc.subject.meshTranscriptional Activationen_HK
dc.subject.meshYeastsen_HK
dc.subject.meshp300-CBP Transcription Factors - metabolism - pharmacologyen_HK
dc.titleInteractions with p300 enhance transcriptional activation by the PDZ-domain coactivator Bridge-1en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-0795&volume=187&spage=283&epage=292&date=2005&atitle=Interactions+with+p300+enhance+transcriptional+activation+by+the+PDZ-domain+coactivator+Bridge-1.en_HK
dc.identifier.emailYao, KM:kmyao@hku.hken_HK
dc.identifier.authorityYao, KM=rp00344en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1677/joe.1.06305en_HK
dc.identifier.pmid16293776en_HK
dc.identifier.scopuseid_2-s2.0-28044439856en_HK
dc.identifier.hkuros114657en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-28044439856&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume187en_HK
dc.identifier.issue2en_HK
dc.identifier.spage283en_HK
dc.identifier.epage292en_HK
dc.identifier.isiWOS:000233666900011-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLee, JH=37960927200en_HK
dc.identifier.scopusauthoridVolinic, JL=9437397700en_HK
dc.identifier.scopusauthoridBanz, C=6603271115en_HK
dc.identifier.scopusauthoridYao, KM=7403234578en_HK
dc.identifier.scopusauthoridThomas, MK=7404754193en_HK

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