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Article: Interactions with p300 enhance transcriptional activation by the PDZ-domain coactivator Bridge-1
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TitleInteractions with p300 enhance transcriptional activation by the PDZ-domain coactivator Bridge-1
 
AuthorsLee, JH1
Volinic, JL1
Banz, C1
Yao, KM2
Thomas, MK1
 
Issue Date2005
 
PublisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.org
 
CitationJournal Of Endocrinology, 2005, v. 187 n. 2, p. 283-292 [How to Cite?]
DOI: http://dx.doi.org/10.1677/joe.1.06305
 
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.
 
ISSN0022-0795
2013 Impact Factor: 3.586
2013 SCImago Journal Rankings: 1.736
 
DOIhttp://dx.doi.org/10.1677/joe.1.06305
 
ISI Accession Number IDWOS:000233666900011
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLee, JH
 
dc.contributor.authorVolinic, JL
 
dc.contributor.authorBanz, C
 
dc.contributor.authorYao, KM
 
dc.contributor.authorThomas, MK
 
dc.date.accessioned2010-09-06T06:03:08Z
 
dc.date.available2010-09-06T06:03:08Z
 
dc.date.issued2005
 
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.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationJournal Of Endocrinology, 2005, v. 187 n. 2, p. 283-292 [How to Cite?]
DOI: http://dx.doi.org/10.1677/joe.1.06305
 
dc.identifier.doihttp://dx.doi.org/10.1677/joe.1.06305
 
dc.identifier.epage292
 
dc.identifier.hkuros114657
 
dc.identifier.isiWOS:000233666900011
 
dc.identifier.issn0022-0795
2013 Impact Factor: 3.586
2013 SCImago Journal Rankings: 1.736
 
dc.identifier.issue2
 
dc.identifier.openurl
 
dc.identifier.pmid16293776
 
dc.identifier.scopuseid_2-s2.0-28044439856
 
dc.identifier.spage283
 
dc.identifier.urihttp://hdl.handle.net/10722/68286
 
dc.identifier.volume187
 
dc.languageeng
 
dc.publisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.org
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofJournal of Endocrinology
 
dc.relation.referencesReferences in Scopus
 
dc.rightsJournal of Endocrinology. Copyright © Society for Endocrinology.
 
dc.subject.meshAdenovirus E1A Proteins - pharmacology
 
dc.subject.meshAnimals
 
dc.subject.meshBlotting, Western
 
dc.subject.meshCells, Cultured
 
dc.subject.meshDiabetes Mellitus, Type 1 - metabolism
 
dc.subject.meshDose-Response Relationship, Drug
 
dc.subject.meshGene Deletion
 
dc.subject.meshGlutathione Transferase - metabolism
 
dc.subject.meshHelix-Loop-Helix Motifs
 
dc.subject.meshHistone Deacetylase Inhibitors
 
dc.subject.meshHydroxamic Acids - pharmacology
 
dc.subject.meshImmunoprecipitation
 
dc.subject.meshInsulin - metabolism
 
dc.subject.meshMutagenesis, Site-Directed
 
dc.subject.meshPoint Mutation
 
dc.subject.meshProteasome Endopeptidase Complex
 
dc.subject.meshProtein Structure, Tertiary
 
dc.subject.meshProteins - genetics - metabolism
 
dc.subject.meshTranscription, Genetic
 
dc.subject.meshTranscriptional Activation
 
dc.subject.meshYeasts
 
dc.subject.meshp300-CBP Transcription Factors - metabolism - pharmacology
 
dc.titleInteractions with p300 enhance transcriptional activation by the PDZ-domain coactivator Bridge-1
 
dc.typeArticle
 
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Author Affiliations
  1. Massachusetts General Hospital
  2. The University of Hong Kong