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Article: Interactions between XIAP associated factor 1 and a nuclear co-activator, CBP, in colon cancer cells
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TitleInteractions between XIAP associated factor 1 and a nuclear co-activator, CBP, in colon cancer cells
 
AuthorsSun, Y2 1
Qiao, L1
Zou, B1
Xia, HHX1
Gu, Q1
Ma, J1
Lin, MCM1
Zhu, Q2
Zhu, S1
Dai, Y1
Wong, BCY1
 
KeywordscAMP response element-binding protein
Colon cancer
XIAP-associated factor 1
 
Issue Date2008
 
PublisherS Karger AG. The Journal's web site is located at http://www.karger.com/DIG
 
CitationDigestion, 2008, v. 77 n. 2, p. 79-86 [How to Cite?]
DOI: http://dx.doi.org/10.1159/000121441
 
AbstractBackground/Aims: XIAP-associated factor 1 (XAF1) is a nuclear protein. CBP, the cAMP response element binding protein (CREB)-binding protein, plays an important role as a multifunctional transcriptional co-activator. In this investigation, we aimed to study the putative interaction between XAF1 and CBP in colon cancer cells. Methods: Expressions of XAF1 and CBP were detected by Western blot and RT-PCR. The interaction between XAF1 and CBP was investigated by the glutathione S-transferase (GST) pull-down assay, colocalization and co-immunoprecipitation analysis. Cell proliferation was examined by cell number counting. Results: Both XAF1 and CBP were co-localized in the nuclei of colon cancer cells and they demonstrated a physical interaction, as revealed by GST pull-down assay and co-immunoprecipitation analysis. CBP I peptide (residues 1-1098) was the interacting domain for XAF1 binding. The functional implication of the interaction between XAF1 and CBP was demonstrated by the finding that cell growth inhibition by XAF1 was potentiated by cotransfection with CBP. Furthermore, a reporter assay demonstrated that cotransfection with XAF1 and CBP led to marked reduction in phorbol ester 12-O-tetradecanoylphorbol-13-acetate (PMA)-stimulated adaptor-related protein complex 1 activity. Conclusions: CBP is a novel binding partner of XAF1, and the interaction between XAF1 and CBP and their functional consequence were mediated by adaptor-related protein complex 1. Copyright © 2008 S. Karger AG.
 
ISSN0012-2823
2012 Impact Factor: 1.94
2012 SCImago Journal Rankings: 0.833
 
DOIhttp://dx.doi.org/10.1159/000121441
 
ISI Accession Number IDWOS:000254893300003
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorSun, Y
 
dc.contributor.authorQiao, L
 
dc.contributor.authorZou, B
 
dc.contributor.authorXia, HHX
 
dc.contributor.authorGu, Q
 
dc.contributor.authorMa, J
 
dc.contributor.authorLin, MCM
 
dc.contributor.authorZhu, Q
 
dc.contributor.authorZhu, S
 
dc.contributor.authorDai, Y
 
dc.contributor.authorWong, BCY
 
dc.date.accessioned2010-09-06T06:20:22Z
 
dc.date.available2010-09-06T06:20:22Z
 
dc.date.issued2008
 
dc.description.abstractBackground/Aims: XIAP-associated factor 1 (XAF1) is a nuclear protein. CBP, the cAMP response element binding protein (CREB)-binding protein, plays an important role as a multifunctional transcriptional co-activator. In this investigation, we aimed to study the putative interaction between XAF1 and CBP in colon cancer cells. Methods: Expressions of XAF1 and CBP were detected by Western blot and RT-PCR. The interaction between XAF1 and CBP was investigated by the glutathione S-transferase (GST) pull-down assay, colocalization and co-immunoprecipitation analysis. Cell proliferation was examined by cell number counting. Results: Both XAF1 and CBP were co-localized in the nuclei of colon cancer cells and they demonstrated a physical interaction, as revealed by GST pull-down assay and co-immunoprecipitation analysis. CBP I peptide (residues 1-1098) was the interacting domain for XAF1 binding. The functional implication of the interaction between XAF1 and CBP was demonstrated by the finding that cell growth inhibition by XAF1 was potentiated by cotransfection with CBP. Furthermore, a reporter assay demonstrated that cotransfection with XAF1 and CBP led to marked reduction in phorbol ester 12-O-tetradecanoylphorbol-13-acetate (PMA)-stimulated adaptor-related protein complex 1 activity. Conclusions: CBP is a novel binding partner of XAF1, and the interaction between XAF1 and CBP and their functional consequence were mediated by adaptor-related protein complex 1. Copyright © 2008 S. Karger AG.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationDigestion, 2008, v. 77 n. 2, p. 79-86 [How to Cite?]
DOI: http://dx.doi.org/10.1159/000121441
 
dc.identifier.doihttp://dx.doi.org/10.1159/000121441
 
dc.identifier.epage86
 
dc.identifier.hkuros141164
 
dc.identifier.isiWOS:000254893300003
 
dc.identifier.issn0012-2823
2012 Impact Factor: 1.94
2012 SCImago Journal Rankings: 0.833
 
dc.identifier.issue2
 
dc.identifier.openurl
 
dc.identifier.pmid18362468
 
dc.identifier.scopuseid_2-s2.0-42349113243
 
dc.identifier.spage79
 
dc.identifier.urihttp://hdl.handle.net/10722/70170
 
dc.identifier.volume77
 
dc.languageeng
 
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/DIG
 
dc.publisher.placeSwitzerland
 
dc.relation.ispartofDigestion
 
dc.relation.referencesReferences in Scopus
 
dc.rightsDigestion. Copyright © S Karger AG.
 
dc.subject.meshCREB-Binding Protein - genetics - metabolism
 
dc.subject.meshCarcinoma - metabolism
 
dc.subject.meshCell Proliferation
 
dc.subject.meshColonic Neoplasms - metabolism
 
dc.subject.meshGene Expression
 
dc.subject.meshGlutathione Transferase
 
dc.subject.meshHCT116 Cells
 
dc.subject.meshHT29 Cells
 
dc.subject.meshHumans
 
dc.subject.meshImmunoprecipitation
 
dc.subject.meshIntracellular Signaling Peptides and Proteins
 
dc.subject.meshNeoplasm Proteins - genetics - metabolism
 
dc.subject.meshTranscriptional Activation
 
dc.subject.meshp300-CBP Transcription Factors - metabolism
 
dc.subjectcAMP response element-binding protein
 
dc.subjectColon cancer
 
dc.subjectXIAP-associated factor 1
 
dc.titleInteractions between XIAP associated factor 1 and a nuclear co-activator, CBP, in colon cancer cells
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. Shanghai Jiaotong University