Evidence map›Paper›PMID 17762865›Full record

ArticleThe EMBO journal2007

SUMO-targeted ubiquitin ligases in genome stability.

John Prudden, Stephanie Pebernard, Grazia Raffa, Daniela A Slavin, J Jefferson P Perry, John A Tainer, Clare H McGowan, Michael N Boddy

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 208 papers.

0numbers the graph read from it
0cells of the map it votes in
208citing papers in PubMed
11.4field-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

208 citing papers in PubMed, 334 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Immune regulation by the SUMO family.Nature reviews. Immunology · 2025
    Review
  11. Synthesizing Defined Ubiquitin-Modified SUMO Dimers.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

148 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

8 authors at 4 institutions in 3 countries.

John PruddenDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Stephanie Pebernard
Grazia Raffa
Daniela A Slavin
J Jefferson P Perry
John A Tainer
Clare H McGowan
Michael N Boddy
Scripps Research Institute · USAmrita Vishwa Vidyapeetham · INLawrence Berkeley National Laboratory · USSapienza University of Rome · IT

Funding

Studies of the Rad60-Smc5-Smc6 DNA Repair ComplexR01GM068608 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BODDY, MICHAEL N · 2003 to 2020
$6.2M
DNA Repair and Checkpoint Interactions in MammalsR01CA095114 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI MCGOWAN, CLARE H · 2003 to 2008
$1.7M
NCI NIH HHS CA095114NCI NIH HHS R01 CA095114NIGMS NIH HHS GM068608NIGMS NIH HHS R01 GM068608
6 · The paper itself

Abstract

We identify the SUMO-Targeted Ubiquitin Ligase (STUbL) family of proteins and propose that STUbLs selectively ubiquitinate sumoylated proteins and proteins that contain SUMO-like domains (SLDs). STUbL recruitment to sumoylated/SLD proteins is mediated by tandem SUMO interaction motifs (SIMs) within the STUbLs N-terminus. STUbL-mediated ubiquitination maintains sumoylation pathway homeostasis by promoting target protein desumoylation and/or degradation. Thus, STUbLs establish a novel mode of communication between the sumoylation and ubiquitination pathways. STUbLs are evolutionarily conserved and include: Schizosaccharomyces pombe Slx8-Rfp (founding member), Homo sapiens RNF4, Dictyostelium discoideum MIP1 and Saccharomyces cerevisiae Slx5-Slx8. Cells lacking Slx8-Rfp accumulate sumoylated proteins, display genomic instability, and are hypersensitive to genotoxic stress. These phenotypes are suppressed by deletion of the major SUMO ligase Pli1, demonstrating the specificity of STUbLs as regulators of sumoylated proteins. Notably, human RNF4 expression restores SUMO pathway homeostasis in fission yeast lacking Slx8-Rfp, underscoring the evolutionary functional conservation of STUbLs. The DNA repair factor Rad60 and its human homolog NIP45, which contain SLDs, are candidate STUbL targets. Consistently, Rad60 and Slx8-Rfp mutants have similar DNA repair defects.

Indexed as

Genomic InstabilityAdaptation, PhysiologicalAmino Acid MotifsAmino Acid SequenceConserved SequenceDNA DamageDNA RepairDNA ReplicationEvolution, MolecularGene DeletionHomeostasisHumansMicrobial ViabilityModels, BiologicalMolecular Sequence DataMutagensMutagensSchizosaccharomyces pombe ProteinsSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating Enzymes

Identifiers

PMID17762865
PMCPMC2230673
OpenAlexW2044287615

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.