2. Academic Validation
  3. SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies

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

  • Sci Rep. 2016 May 23;6:26509. doi: 10.1038/srep26509.
Ya-Chen Liang 1,  Chia-Chin Lee 1,  Ya-Li Yao 2,  Chien-Chen Lai 1,  M Lienhard Schmitz 3,  Wen-Ming Yang 1
Affiliations

Affiliations

  • 1 Institute of Molecular Biology, National Chung Hsing University, Taichung 40227, Taiwan.
  • 2 Department of Biotechnology, Asia University, Taichung 41354, Taiwan.
  • 3 Institute of Biochemistry, Medical Faculty, Friedrichstrasse 24, Justus-Liebig-University, 35392 Giessen, Germany.
PMID: 27211601 DOI: 10.1038/srep26509
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-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.

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