Evidence map›Paper›PMID 21079245›Full record

ArticleThe Journal of cell biology2010

PIASy-dependent SUMOylation regulates DNA topoisomerase IIalpha activity.

Hyunju Ryu, Maiko Furuta, Donald Kirkpatrick, Steven P Gygi, Yoshiaki Azuma

Abstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
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

52 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. PARP1 UFMylation ensures the stability of stalled replication forks.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. SUMO: A Swiss Army Knife for Eukaryotic Topoisomerases.Frontiers in molecular biosciences · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Molecular mechanisms of topoisomerase 2 DNA-protein crosslink resolution.Cellular and molecular life sciences : CMLS · 2020
    Review
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

5 authors.

Hyunju RyuDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Maiko Furuta
Donald Kirkpatrick
Steven P Gygi
Yoshiaki Azuma

Funding

WEIGHT CONTROL, CELL SIGNALING AND CANCER PREVENTIONP20RR015563 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI ZUFFEREY, RACHEL · 2000 to 2009
$20.1M
New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
Regulation and function of PIASy mediated mitotic SUMOylation in vertebratesR01GM080278 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI AZUMA, YOSHIAKI · 2007 to 2011
$1.6M
NCRR NIH HHS P20 RR015563NIGMS NIH HHS GM67945NIGMS NIH HHS GM80278NIGMS NIH HHS R01 GM067945NIGMS NIH HHS R01 GM080278
6 · The paper itself

Abstract

DNA topoisomerase IIα (TopoIIα) is an essential chromosome-associated enzyme with activity implicated in the resolution of tangled DNA at centromeres before anaphase onset. However, the regulatory mechanism of TopoIIα activity is not understood. Here, we show that PIASy-mediated small ubiquitin-like modifier 2/3 (SUMO2/3) modification of TopoIIα strongly inhibits TopoIIα decatenation activity. Using mass spectrometry and biochemical analysis, we demonstrate that TopoIIα is SUMOylated at lysine 660 (Lys660), a residue located in the DNA gate domain, where both DNA cleavage and religation take place. Remarkably, loss of SUMOylation on Lys660 eliminates SUMOylation-dependent inhibition of TopoIIα, which indicates that Lys660 SUMOylation is critical for PIASy-mediated inhibition of TopoIIα activity. Together, our findings provide evidence for the regulation of TopoIIα activity on mitotic chromosomes by SUMOylation. Therefore, we propose a novel mechanism for regulation of centromeric DNA catenation during mitosis by PIASy-mediated SUMOylation of TopoIIα.

Indexed as

Amino Acid SequenceAnimalsAntigens, NeoplasmDNA-Binding ProteinsDNA, CatenatedDNA Topoisomerases, Type IIMolecular ChaperonesMolecular Sequence DataNuclear Pore Complex ProteinsProtein Inhibitors of Activated STATRecombinant Fusion ProteinsSmall Ubiquitin-Related Modifier ProteinsSumoylationXenopus laevisXenopus ProteinsAntigens, NeoplasmDNA-Binding ProteinsDNA, CatenatedDNA Topoisomerases, Type IIMolecular ChaperonesNuclear Pore Complex ProteinsProtein Inhibitors of Activated STATran-binding protein 2Recombinant Fusion ProteinsSmall Ubiquitin-Related Modifier ProteinsXenopus Proteins

Identifiers

PMID21079245
PMCPMC2983052

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.