Evidence map›Paper›PMID 20516210›Full record

ArticleMolecular and cellular biology2010

Wss1 is a SUMO-dependent isopeptidase that interacts genetically with the Slx5-Slx8 SUMO-targeted ubiquitin ligase.

Janet R Mullen, Chi-Fu Chen, Steven J Brill

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  6. Article
  7. Targeting DNA-Protein CrosslinksFrontiers in molecular biosciences · 2022
    Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. DNA- and DNA-Protein-Crosslink Repair in Plants.International journal of molecular sciences · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Janet R MullenDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA.
Chi-Fu Chen
Steven J Brill
Rutgers, The State University of New Jersey · US

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

Protein sumoylation plays an important but poorly understood role in controlling genome integrity. In Saccharomyces cerevisiae, the Slx5-Slx8 SUMO-targeted Ub ligase appears to be needed to ubiquitinate sumoylated proteins that arise in the absence of the Sgs1 DNA helicase. WSS1, a high-copy-number suppressor of a mutant SUMO, was implicated in this pathway because it shares phenotypes with SLX5-SLX8 mutants, including a wss1Delta sgs1Delta synthetic-fitness defect. Here we show that Wss1, a putative metalloprotease, physically binds SUMO and displays in vitro isopeptidase activity on poly-SUMO chains. Like that of SLX5, overexpression of WSS1 suppresses sgs1Delta slx5Delta lethality and the ulp1ts growth defect. Interestingly, although Wss1 is relatively inactive on ubiquitinated substrates and poly-Ub chains, it efficiently deubiquitinates a Ub-SUMO isopeptide conjugate and a Ub-SUMO fusion protein. Wss1 was further implicated in Ub metabolism on the basis of its physical association with proteasomal subunits. The results suggest that Wss1 is a SUMO-dependent isopeptidase that acts on sumoylated substrates as they undergo proteasomal degradation.

Indexed as

Carbon-Nitrogen LyasesDNA HelicasesProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalSaccharomyces cerevisiaeUbiquitinCarbon-Nitrogen LyasesDNA HelicasesisopeptidaseProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID20516210
PMCPMC2916399
OpenAlexW2125945836

What OpenQuestion holds

Textmetadata
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.