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유전체항상성연구단
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Sumoylation of the histone demethylase KDM4A is required for binding to tumor suppressor p53 in HCT116 colon cancer cell lines

DC Field Value Language
dc.contributor.authorYu, SE-
dc.contributor.authorSu Hyung Park-
dc.contributor.authorJang, YK-
dc.date.available2018-07-18T02:07:50Z-
dc.date.created2018-04-16-
dc.date.issued2018-01-
dc.identifier.issn1976-8354-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/4743-
dc.description.abstractThe histone demethylase lysine-specific demethylase 4A (KDM4A/Jmjd2A) has diverse functions, including involvement in gene regulation and cell cycle, and plays an oncogenic role in cancer cells. The modulation of KDM4A through post-translational modifications remains unclear. Here, we show that small ubiquitin-like modifier (SUMO) 1-mediated modification of KDM4A was required for interaction with tumor suppressor p53. Our data revealed that KDM4A is mainly sumoylated at lysine residue 471. However, the SUMO modification resulted in little change in subcellular localization, demethylase activity, or protein stability of KMD4A. Intriguingly, co-immunoprecipitation data revealed that sumoylation-defective mutants of KDM4A had a lower binding ability with p53 compared to that of wild-type KDM4A, suggesting a positive role for sumoylation in the interaction between KDM4A and p53. Together, these data suggest that KDM4A is post-translationally modified by SUMO, and this sumoylation may be a novel regulatory switch for controlling the interplay between KDM4A and p53 © 2018 The Author(s).-
dc.language영어-
dc.publisherTAYLOR & FRANCIS LTD-
dc.titleSumoylation of the histone demethylase KDM4A is required for binding to tumor suppressor p53 in HCT116 colon cancer cell lines-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000424135500004-
dc.identifier.scopusid2-s2.0-85041002945-
dc.identifier.rimsid62989-
dc.date.tcdate2018-10-01-
dc.contributor.affiliatedAuthorSu Hyung Park-
dc.identifier.doi10.1080/19768354.2018.1426628-
dc.identifier.bibliographicCitationANIMAL CELLS AND SYSTEMS, v.22, no.1, pp.22 - 28-
dc.relation.isPartOfANIMAL CELLS AND SYSTEMS-
dc.citation.titleANIMAL CELLS AND SYSTEMS-
dc.citation.volume22-
dc.citation.number1-
dc.citation.startPage22-
dc.citation.endPage28-
dc.date.scptcdate2018-10-01-
dc.description.scptc0-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.relation.journalWebOfScienceCategoryZoology-
dc.subject.keywordPlusLYSINE METHYLATION-
dc.subject.keywordPlusPHOSPHORYLATION-
dc.subject.keywordPlusDEGRADATION-
dc.subject.keywordPlusSUMO-
dc.subject.keywordAuthorColon cancer cells-
dc.subject.keywordAuthorhistone demethylase-
dc.subject.keywordAuthorKDM4A-
dc.subject.keywordAuthorp53-
dc.subject.keywordAuthorsumoylation-
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > 1. Journal Papers (저널논문)
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