Evidence map›Paper›PMID 17762864›Full record

ArticleThe EMBO journal2007

Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins.

Huaiyu Sun, Joel D Leverson, Tony Hunter

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 188 papers.

0numbers the graph read from it
0cells of the map it votes in
188citing papers in PubMed
11.1field-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

188 citing papers in PubMed, 292 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Immune regulation by the SUMO family.Nature reviews. Immunology · 2025
    Review
  11. SUMO Antibody Validation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. SUMOylation-mediated PSME3-20Science advances · 2023
    Article
  19. 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
  20. Article

128 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

3 authors at 1 institution in 1 country.

Huaiyu SunMolecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
Joel D Leverson
Tony Hunter
Salk Institute for Biological Studies · US

Funding

SOMATIC CELL CYCLE REGULATION BY PHOSPHORYLATIONR01CA080100 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI HUNTER, TONY R. · 1999 to 2018
$13.1M
SIGNAL TRANSDUCTION BY TYROSINE PHOSPHORYLATIONR01CA082683 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI HUNTER, TONY R. · 1999 to 2019
$12.2M
NCI NIH HHS CA80100NCI NIH HHS CA82683NCI NIH HHS R01 CA080100NCI NIH HHS R01 CA082683
6 · The paper itself

Abstract

The function of small ubiquitin-like modifier (SUMO)-binding proteins is key to understanding how SUMOylation regulates cellular processes. We identified two related Schizosaccharomyces pombe proteins, Rfp1 and Rfp2, each having an N-terminal SUMO-interacting motif (SIM) and a C-terminal RING-finger domain. Genetic analysis shows that Rfp1 and Rfp2 have redundant functions; together, they are essential for cell growth and genome stability. Mammalian RNF4, an active ubiquitin E3 ligase, is an orthologue of Rfp1/Rfp2. Rfp1 and Rfp2 lack E3 activity but recruit Slx8, an active RING-finger ubiquitin ligase, through a RING-RING interaction, to form a functional E3. RNF4 complements the growth and genomic stability defects of rfp1rfp2, slx8, and rfp1rfp2slx8 mutant cells. Both the Rfp-Slx8 complex and RNF4 specifically ubiquitylate artificial SUMO-containing substrates in vitro in a SUMO binding-dependent manner. SUMOylated proteins accumulate in rfp1rfp2 double-null cells, suggesting that Rfp/Slx8 proteins may promote ubiquitin-dependent degradation of SUMOylated targets. Hence, we describe a family of SIM-containing RING-finger proteins that potentially regulates eukaryotic genome stability through linking SUMO-interaction with ubiquitin conjugation.

Indexed as

Evolution, MolecularMultigene FamilyAmino Acid MotifsAmino Acid SequenceAnimalsCarrier ProteinsCell Cycle ProteinsEukaryotic CellsGenomic InstabilityMiceMolecular Sequence DataNuclear ProteinsProtein BindingProtein TransportSchizosaccharomycesSchizosaccharomyces pombe ProteinsCarrier ProteinsCell Cycle ProteinsNuclear ProteinsRnf4 protein, mouseRpf1 protein, S pombeRpf2 protein, S pombeSchizosaccharomyces pombe ProteinsSlx8 protein, S pombeSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID17762864
PMCPMC2230674
OpenAlexW1994218254

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.