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
2011 Impact Factor: 3.548
2011 SCImago Journal Rankings: 0.322
DOIhttp://dx.doi.org/10.1677/joe.1.06305
ISI Accession Number IDWOS:000233666900011
ReferencesReferences in Scopus
DC Field
Value
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
2011 Impact Factor: 3.548
2011 SCImago Journal Rankings: 0.322
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
Author Affiliations
  1. Massachusetts General Hospital
  2. The University of Hong Kong