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SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies.

ABSTRACT: 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-RAR? 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.

SUBMITTER: Liang YC

PROVIDER: S-EPMC4876461 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

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SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies.

Liang Ya-Chen YC Lee Chia-Chin CC Yao Ya-Li YL Lai Chien-Chen CC Schmitz M Lienhard ML Yang Wen-Ming WM

Scientific reports 20160523

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 ly ...[more]

PMID: 27211601

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