Evidence map›Paper›PMID 25425640›Full record

ArticleThe Journal of biological chemistry2015

SUMOylation attenuates human β-arrestin 2 inhibition of IL-1R/TRAF6 signaling.

Ning Xiao, Hui Li, Wenhan Mei, Jinke Cheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Pharmacological reviews · 2023
    Review
  4. Article
  5. Article
  6. G Protein-Coupled Receptor Systems and Their Role in Cellular Senescence.Computational and structural biotechnology journal · 2019
    Review
  7. Article
  8. Review
  9. 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

4 authors at 4 institutions in 1 country.

Ning XiaoFrom the Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, State Key Laboratory of Oncogenes and Related Genes in Shanghai Cancer Institute, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China and.
Hui Lithe Key Laboratory of Pediatric Hematology and Oncology, Ministry of Health, Pediatric Translational Medicine Institute, Shanghai Jiao Tong University School of Medicine, Shanghai 200127, China.
Wenhan MeiFrom the Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, jymeiwh@shsmu.edu.cn.
Jinke ChengFrom the Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, State Key Laboratory of Oncogenes and Related Genes in Shanghai Cancer Institute, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China and jkcheng@shsmu.edu.cn.
Center for Excellence in Molecular Cell Science · CNShanghai Cancer Institute · CNShanghai Jiao Tong University · CNState Key Laboratory of Oncogene and Related Genes · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Arrestin 2 as an adaptor plays a role in the regulation of receptor desensitization, trafficking, and signaling. Bovine β-arrestin 2 has been shown to be SUMOylated on the lysine 400 residue, which links it to the endocytosis of the β2-adrenergic receptor. Here we identify a major SUMOylation site, lysine 295, on human β-arrestin 2. SUMOylation on this site attenuates β-arrestin 2 binding to TRAF6, then enhances TRAF6 oligomerization and autoubiquitination, and consequently leads to the increase of TRAF6-mediated NF-κB/AP-1 activation. We further determine SENP1 as a specific de-SUMOylation protease that can reverse the SUMOylation of β-arrestin 2-mediated processes. Our study reveals SUMOylation as a novel mechanism in the regulation of β-arrestin 2-mediated IL-1R/TRAF6 signaling.

Indexed as

SumoylationAnimalsArrestinsbeta-Arrestin 2beta-ArrestinsEndocytosisEnzyme-Linked Immunosorbent AssayHEK293 CellsHumansLysineMCF-7 CellsMiceProtein BindingReceptors, Interleukin-1Signal TransductionTNF Receptor-Associated Factor 6ARRB2 protein, humanArrb2 protein, mouseArrestinsbeta-Arrestin 2beta-ArrestinsLysineReceptors, Interleukin-1TNF Receptor-Associated Factor 6Transcription Factor AP-1UbiquitinArrestinArrestin Cell SignalingCell SignalingIL-1Small Ubiquitin-like Modifier (SUMO)Ubiquitylation (Ubiquitination)

Identifiers

PMID25425640
PMCPMC4303650
OpenAlexW2016988195

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.