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Article: Interactions between XIAP associated factor 1 and a nuclear co-activator, CBP, in colon cancer cells

TitleInteractions between XIAP associated factor 1 and a nuclear co-activator, CBP, in colon cancer cells
Authors
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
Citation
Digestion, 2008, v. 77 n. 2, p. 79-86 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/70170
ISSN
2021 Impact Factor: 3.672
2020 SCImago Journal Rankings: 0.882
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSun, Yen_HK
dc.contributor.authorQiao, Len_HK
dc.contributor.authorZou, Ben_HK
dc.contributor.authorXia, HHXen_HK
dc.contributor.authorGu, Qen_HK
dc.contributor.authorMa, Jen_HK
dc.contributor.authorLin, MCMen_HK
dc.contributor.authorZhu, Qen_HK
dc.contributor.authorZhu, Sen_HK
dc.contributor.authorDai, Yen_HK
dc.contributor.authorWong, BCYen_HK
dc.date.accessioned2010-09-06T06:20:22Z-
dc.date.available2010-09-06T06:20:22Z-
dc.date.issued2008en_HK
dc.identifier.citationDigestion, 2008, v. 77 n. 2, p. 79-86en_HK
dc.identifier.issn0012-2823en_HK
dc.identifier.urihttp://hdl.handle.net/10722/70170-
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.en_HK
dc.languageengen_HK
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/DIGen_HK
dc.relation.ispartofDigestionen_HK
dc.rightsDigestion. Copyright © S Karger AG.en_HK
dc.subjectcAMP response element-binding proteinen_HK
dc.subjectColon canceren_HK
dc.subjectXIAP-associated factor 1en_HK
dc.subject.meshCREB-Binding Protein - genetics - metabolismen_HK
dc.subject.meshCarcinoma - metabolismen_HK
dc.subject.meshCell Proliferationen_HK
dc.subject.meshColonic Neoplasms - metabolismen_HK
dc.subject.meshGene Expressionen_HK
dc.subject.meshGlutathione Transferaseen_HK
dc.subject.meshHCT116 Cellsen_HK
dc.subject.meshHT29 Cellsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshImmunoprecipitationen_HK
dc.subject.meshIntracellular Signaling Peptides and Proteinsen_HK
dc.subject.meshNeoplasm Proteins - genetics - metabolismen_HK
dc.subject.meshTranscriptional Activationen_HK
dc.subject.meshp300-CBP Transcription Factors - metabolismen_HK
dc.titleInteractions between XIAP associated factor 1 and a nuclear co-activator, CBP, in colon cancer cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0012-2823&volume=77&spage=79&epage=86&date=2008&atitle=Interactions+between+XIAP+Associated+Factor+1+and+a+Nuclear+Co-Activator,+CBP,+in+Colon+Cancer+Cellsen_HK
dc.identifier.emailQiao, L: lq8688@hotmail.comen_HK
dc.identifier.emailLin, MCM: mcllin@hkucc.hku.hken_HK
dc.identifier.emailWong, BCY: bcywong@hku.hken_HK
dc.identifier.authorityQiao, L=rp00513en_HK
dc.identifier.authorityLin, MCM=rp00746en_HK
dc.identifier.authorityWong, BCY=rp00429en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1159/000121441en_HK
dc.identifier.pmid18362468-
dc.identifier.scopuseid_2-s2.0-42349113243en_HK
dc.identifier.hkuros141164en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-42349113243&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume77en_HK
dc.identifier.issue2en_HK
dc.identifier.spage79en_HK
dc.identifier.epage86en_HK
dc.identifier.isiWOS:000254893300003-
dc.publisher.placeSwitzerlanden_HK
dc.identifier.scopusauthoridSun, Y=12776261000en_HK
dc.identifier.scopusauthoridQiao, L=7202151719en_HK
dc.identifier.scopusauthoridZou, B=35228257300en_HK
dc.identifier.scopusauthoridXia, HHX=8757161400en_HK
dc.identifier.scopusauthoridGu, Q=24469982400en_HK
dc.identifier.scopusauthoridMa, J=35275386200en_HK
dc.identifier.scopusauthoridLin, MCM=7404816359en_HK
dc.identifier.scopusauthoridZhu, Q=36242678700en_HK
dc.identifier.scopusauthoridZhu, S=7404391208en_HK
dc.identifier.scopusauthoridDai, Y=7401512993en_HK
dc.identifier.scopusauthoridWong, BCY=7402023340en_HK
dc.identifier.issnl0012-2823-

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