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dc.contributor.authorYou, Dong-Joo-
dc.contributor.authorPark, Cho Rong-
dc.contributor.authorFurlong, Michael-
dc.contributor.authorKoo, Okjae-
dc.contributor.authorLee, Cheolju-
dc.contributor.authorAlm, Curie-
dc.contributor.authorSeong, Jae Young-
dc.contributor.authorHwang, Jong-Ik-
dc.date.accessioned2024-01-20T05:34:16Z-
dc.date.available2024-01-20T05:34:16Z-
dc.date.created2021-09-05-
dc.date.issued2015-11-
dc.identifier.issn0898-6568-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/124796-
dc.description.abstractI kappa B kinases (IKKs) are a therapeutic target due to their crucial roles in various biological processes, including the immune response, the stress response, and tumor development. IKKs integrate various upstream signals that activate NF-kappa B by phosphorylating I kappa B and also regulate many proteins related to cell growth and metabolism. Although they function as a heteromeric complex comprised of kinase subunits and an adaptor, these kinases produce distinct cellular responses by phosphorylating different target molecules, suggesting that they may also be regulated in a subtype-specific manner. In this study, arfaptin 2 was identified as an IKK beta-specific binding partner. Interestingly, arfaptin 2 also interacted with NEMO. Domain mapping studies revealed that the C-terminal region, including the IKK beta HLH domain and the first coiled-coil NEMO region were respectively required for interactions with the arfaptin 2 N-terminal flexible region. Overexpression of arfaptin 2 inhibited tumor necrosis factor (TNF)-alpha-stimulated nuclear factor-kappa B (NF-kappa B) signaling, whereas downregulation of arfaptin 2 by small interfering RNA enhanced NF-kappa B activity. Dimerization of arfaptin 2 through the Bin-Amphiphysin-Rvs domain may be essential to inhibit activation of NF-kappa B through multimodal interactions with IKK beta s or IKK beta/NEMO, as ectopic expression of the arfaptin 2 fragment responsible for IKK interactions did not change TNF alpha-stimulated NF-kappa B activation. These data indicate that arfaptin 2 is the first molecule to regulate NF-kappa B signaling by interacting with the functional IKK complex but not by direct inhibiting IKK beta phosphorylation. (C) 2015 Elsevier Inc. All rights reserved.-
dc.languageEnglish-
dc.publisherELSEVIER SCIENCE INC-
dc.subjectRAC1-INTERACTING PROTEIN-
dc.subjectACTIVATION-
dc.subjectPHOSPHORYLATION-
dc.subjectCOMPLEX-
dc.subjectNEMO-
dc.subjectTRANSCRIPTION-
dc.subjectBINDING-
dc.subjectTUMORIGENESIS-
dc.subjectPATHWAYS-
dc.subjectCANCER-
dc.titleDimer of arfaptin 2 regulates NF-kappa B signaling by interacting with IKK beta/NEMO and inhibiting IKK beta kinase activity-
dc.typeArticle-
dc.identifier.doi10.1016/j.cellsig.2015.08.012-
dc.description.journalClass1-
dc.identifier.bibliographicCitationCELLULAR SIGNALLING, v.27, no.11, pp.2173 - 2181-
dc.citation.titleCELLULAR SIGNALLING-
dc.citation.volume27-
dc.citation.number11-
dc.citation.startPage2173-
dc.citation.endPage2181-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000361777500004-
dc.identifier.scopusid2-s2.0-84941260687-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.relation.journalResearchAreaCell Biology-
dc.type.docTypeArticle-
dc.subject.keywordPlusRAC1-INTERACTING PROTEIN-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlusPHOSPHORYLATION-
dc.subject.keywordPlusCOMPLEX-
dc.subject.keywordPlusNEMO-
dc.subject.keywordPlusTRANSCRIPTION-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusTUMORIGENESIS-
dc.subject.keywordPlusPATHWAYS-
dc.subject.keywordPlusCANCER-
dc.subject.keywordAuthorI kappa B kinases-
dc.subject.keywordAuthorArfaptin 2-
dc.subject.keywordAuthorNF-kappa B-
dc.subject.keywordAuthorTNF-alpha-
dc.subject.keywordAuthorBAR domain-
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