Evidence map›Paper›PMID 15773819›Full record

ArticleThe Biochemical journal2005

E3 ubiquitin ligase RNF2 interacts with the S6' proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6'.

Sun-Joo Lee, Dongwon Choi, Hyangshuk Rhim, Seongman Kang

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. E3 ubiquitin ligase RNF2 protects polymerase ι from destabilization.Biochimica et biophysica acta. Molecular cell research · 2024
    Article
  3. RNF2 mediates pulmonary fibroblasts activation and proliferation by regulating mTOR and p16-CDK4-Rb1 signaling pathway.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2022
    Article
  4. Article
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  7. Review
  8. Article
  9. Mdm2 facilitates the association of p53 with the proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Article
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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

4 authors at 2 institutions in 1 country.

Sun-Joo LeeGraduate School of Biotechnology, Korea University, 1,5-ka Anam-dong, Seoul 136-701, South Korea.
Dongwon Choi
Hyangshuk Rhim
Seongman Kang
Korea University · KRCatholic University of Korea · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We reported previously that the human RNF2 (RING finger protein 2) protein is an E3 ubiquitin ligase that interacts with the human ubiquitin-conjugating enzyme Hip-2/hE2-25K. In the present study, we show that RNF2 interacts with S6' ATPase, a subunit of the proteasomal 19 S regulatory complex. S6' interacts with RNF2 through its N-terminal RING domain, and RNF2 interacts with S6' through its C-terminal region. Interestingly, the RNF2-S6' interaction increases the ATP hydrolysis activity of the S6' protein. Moreover, S6' ATPase activity is highly increased in the presence of ubiquitinated proteins. The present study suggests that the E3 ubiquitin ligase RNF2 might have a dual function: facilitating the ubiquitination of its target substrates and recruiting the substrates to the proteasome. Furthermore, ATP hydrolysis in the E3/proteasome complex might act as an important signal for the protein degradation pathway.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateCell LineDNA-Binding ProteinsHumansHydrolysisPolycomb Repressive Complex 1Proteasome Endopeptidase ComplexProtein BindingProtein Structure, TertiaryProtein SubunitsSaccharomyces cerevisiaeSignal TransductionSubstrate SpecificityTwo-Hybrid System TechniquesUbiquitin-Protein LigasesAdenosine TriphosphatasesAdenosine TriphosphateDNA-Binding ProteinsPolycomb Repressive Complex 1Proteasome Endopeptidase ComplexProtein SubunitsRNF2 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID15773819
PMCPMC1175123
OpenAlexW2060586155

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.