Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/94769
標題: SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies
作者: Liang, Ya-Chen
Lee, Chia-Chin
Yao, Ya-Li
Lai, Chien-Chen
Schmitz, M Lienhard
Yang, Wen-Ming
楊文明
Project: Scientific reports, Volume 6, Page(s) 26509.
摘要: 
Promyelocytic 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.
URI: http://hdl.handle.net/11455/94769
DOI: 10.1038/srep26509
Appears in Collections:分子生物學研究所

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