SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies
Copyright policy )SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies
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-RARĪ± 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.
- Asian University Taiwan
- Justus Liebig University Giessen Germany
- National Chung Hsing University Taiwan
Cell Nucleus, Lysine, Nuclear Proteins, Sumoylation, Promyelocytic Leukemia Protein, Article, Mice, HEK293 Cells, Gene Expression Regulation, Organ Specificity, Cell Line, Tumor, MCF-7 Cells, NIH 3T3 Cells, Small Ubiquitin-Related Modifier Proteins, Animals, Humans, Protein Isoforms, Cloning, Molecular, K562 Cells, HeLa Cells, Transcription Factors
Cell Nucleus, Lysine, Nuclear Proteins, Sumoylation, Promyelocytic Leukemia Protein, Article, Mice, HEK293 Cells, Gene Expression Regulation, Organ Specificity, Cell Line, Tumor, MCF-7 Cells, NIH 3T3 Cells, Small Ubiquitin-Related Modifier Proteins, Animals, Humans, Protein Isoforms, Cloning, Molecular, K562 Cells, HeLa Cells, Transcription Factors
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