Evidence map›Paper›PMID 27211601›Full record

ArticleScientific reports2016

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

Ya-Chen Liang, Chia-Chin Lee, Ya-Li Yao, Chien-Chen Lai, M Lienhard Schmitz, Wen-Ming Yang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed
10.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

139 citing papers in PubMed, 217 citations in OpenAlex.

  1. Review
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  5. Review
  6. Review
  7. Article
  8. Article
  9. SUMO conjugation to promoter-proximal sequence elements-associated proteins impacts on snRNA transcription.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. The role of SUMOylation in epithelial-mesenchymal transition.Journal of molecular medicine (Berlin, Germany) · 2025
    Review
  11. Immune regulation by the SUMO family.Nature reviews. Immunology · 2025
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  18. Article
  19. Review
  20. Article

79 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Ya-Chen LiangInstitute of Molecular Biology, National Chung Hsing University, Taichung 40227, Taiwan.
Chia-Chin LeeInstitute of Molecular Biology, National Chung Hsing University, Taichung 40227, Taiwan.
Ya-Li YaoDepartment of Biotechnology, Asia University, Taichung 41354, Taiwan.
Chien-Chen LaiInstitute of Molecular Biology, National Chung Hsing University, Taichung 40227, Taiwan.
M Lienhard SchmitzInstitute of Biochemistry, Medical Faculty, Friedrichstrasse 24, Justus-Liebig-University, 35392 Giessen, Germany.
Wen-Ming YangInstitute of Molecular Biology, National Chung Hsing University, Taichung 40227, Taiwan.
National Chung Hsing University · TWAsia University · TWUniversity of Giessen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AnimalsCell Line, TumorCell NucleusCloning, MolecularGene Expression RegulationHEK293 CellsHeLa CellsHumansK562 CellsLysineMCF-7 CellsMiceNIH 3T3 CellsNuclear ProteinsOrgan SpecificityPromyelocytic Leukemia ProteinLysineNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinProtein IsoformsRNF4 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanTranscription FactorsUbiquitins

Identifiers

PMID27211601
PMCPMC4876461
OpenAlexW2402259557

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.