Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/94769
DC FieldValueLanguage
dc.contributor.authorLiang, Ya-Chenzh_TW
dc.contributor.authorLee, Chia-Chinzh_TW
dc.contributor.authorYao, Ya-Lizh_TW
dc.contributor.authorLai, Chien-Chenzh_TW
dc.contributor.authorSchmitz, M Lienhardzh_TW
dc.contributor.authorYang, Wen-Mingzh_TW
dc.contributor.author楊文明zh_TW
dc.date2016-05-23-
dc.date.accessioned2018-03-30T06:21:41Z-
dc.date.available2018-03-30T06:21:41Z-
dc.identifier.urihttp://hdl.handle.net/11455/94769-
dc.description.abstractPromyelocytic leukemia nuclear bodies (PML-NBs) are PML-based nuclear structures that regulate various cellular processes. SUMOylation, the process of covalently conjugating small ubiquitin-like modifiers (SUMOs), is required for both the formation and the disruption of PML-NBs. However, detailed mechanisms of how SUMOylation regulates these processes remain unknown. Here we report that SUMO5, a novel SUMO variant, mediates the growth and disruption of PML-NBs. PolySUMO5 conjugation of PML at lysine 160 facilitates recruitment of PML-NB components, which enlarges PML-NBs. SUMO5 also increases polySUMO2/3 conjugation of PML, resulting in RNF4-mediated disruption of PML-NBs. The acute promyelocytic leukemia oncoprotein PML-RARα blocks SUMO5 conjugation of PML, causing cytoplasmic displacement of PML and disruption of PML-NBs. Our work not only identifies a new member of the SUMO family but also reveals the mechanistic basis of the PML-NB life cycle in human cells.zh_TW
dc.language.isoenzh_TW
dc.relationScientific reports, Volume 6, Page(s) 26509.zh_TW
dc.titleSUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodieszh_TW
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1038/srep26509zh_TW
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
item.openairetypeJournal Article-
item.grantfulltextrestricted-
item.fulltextwith fulltext-
item.cerifentitytypePublications-
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