Evidence map›Paper›PMID 21059884›Full record

ArticleGenetics2011

Genetic evidence that polysumoylation bypasses the need for a SUMO-targeted Ub ligase.

Janet R Mullen, Mukund Das, Steven J Brill

Abstract read
In one paragraph

Article in Genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. DNA- and DNA-Protein-Crosslink Repair in Plants.International journal of molecular sciences · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Function and regulation of SUMO proteases.Nature reviews. Molecular cell biology · 2012
    Review
  20. Article
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

3 authors.

Janet R MullenDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA.
Mukund Das
Steven J Brill

Funding

Genomic Stability and RecQ DNA Helicases in YeastR01GM071268 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI BRILL, STEVEN J. · 2004 to 2012
$2.5M
NIGMS NIH HHS GM071268NIGMS NIH HHS R01 GM071268
6 · The paper itself

Abstract

Saccharomyces cerevisiae cells lacking the Slx5-Slx8 SUMO-targeted Ub ligase display increased levels of sumoylated and polysumoylated proteins, and they are inviable in the absence of the Sgs1 DNA helicase. One explanation for this inviability is that one or more sumoylated proteins accumulate to toxic levels in sgs1Δ slx5Δ cells. To address this possibility, we isolated a second-site suppressor of sgs1Δ slx5Δ synthetic lethality and identified it as an allele of the ULP2 SUMO isopeptidase. The suppressor, ulp2-D623H, behaved like the ulp2Δ allele in its sensitivity to heat, DNA replication stress, and DNA damage. Surprisingly, deletion of ULP2, which is known to promote the accumulation of poly-SUMO chains, suppressed sgs1Δ slx5Δ synthetic lethality and the slx5Δ sporulation defect. Further, ulp2Δ's growth sensitivities were found to be suppressed in ulp2Δ slx5Δ double mutants. This mutual suppression indicates that SLX5-SLX8 and ULP2 interact antagonistically. However, the suppressed strain sgs1Δ slx5Δ ulp2-D623H displayed even higher levels of sumoylated proteins than the corresponding double mutants. Thus, sgs1Δ slx5Δ synthetic lethality cannot be due simply to high levels of bulk sumoylated proteins. We speculate that the loss of ULP2 suppresses the toxicity of the sumoylated proteins that accumulate in slx5Δ-slx8Δ cells by permitting the extension of poly-SUMO chains on specific target proteins. This additional modification might attenuate the activity of the target proteins or channel them into alternative pathways for proteolytic degradation. In support of this latter possibility we find that the WSS1 isopeptidase is required for suppression by ulp2Δ.

Indexed as

AllelesAmino Acid SequenceEndopeptidasesGenes, SuppressorGenomic InstabilityMolecular Sequence DataMutationPhenotypeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSUMO-1 ProteinSumoylationUbiquitin-Protein LigasesEndopeptidasesSaccharomyces cerevisiae ProteinsSlx5 protein, S cerevisiaeSlx8 protein, S cerevisiaeSUMO-1 ProteinUbiquitin-Protein LigasesULP2 protein, S cerevisiaeWSS1 protein, S cerevisiae

Identifiers

PMID21059884
PMCPMC3018298

What OpenQuestion holds

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Registered trials

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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.