Evidence map›Paper›PMID 30224829›Full record

ArticleScientific reports2018

The E3 ubiquitin ligase Trim13 regulates Nur77 stability via casein kinase 2α.

Bin Huang, Han Zhong Pei, Hyeun-Wook Chang, Suk-Hwan Baek

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
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  4. Controversy and multiple roles of the solitary nucleus receptor Nur77 in disease and physiology.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
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  8. Review
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  14. Blocking PPARγ interaction facilitates Nur77 interdiction of fatty acid uptake and suppresses breast cancer progression.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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 1 institution in 1 country.

Bin HuangDepartment of Biochemistry & Molecular Biology, College of Medicine, Yeungnam University, Daegu, South Korea.
Han Zhong PeiDepartment of Biochemistry & Molecular Biology, College of Medicine, Yeungnam University, Daegu, South Korea.
Hyeun-Wook ChangCollege of Pharmacy, Yeungnam University, Gyeongsan, South Korea. hwchang@yu.ac.kr.
Suk-Hwan BaekDepartment of Biochemistry & Molecular Biology, College of Medicine, Yeungnam University, Daegu, South Korea. sbaek@med.yu.ac.kr.
Yeungnam University · KR

Funding

National Research Foundation of Korea (NRF) NRF-2015R1D1A3A01015809
6 · The paper itself

Abstract

Nur77 is a member of the NR4A subfamily of nuclear receptors and has been shown to regulate various biological processes such as apoptosis and inflammation. Here, we show that Nur77 ubiquitination is mediated by the tripartite motif 13 (Trim13), a RING-type E3 ubiquitin ligase. The interaction between Nur77 and Trim13 was confirmed by co-immunoprecipitation. Moreover, we found that Lys539 in Nur77 ubiquitination is targeted for Trim13, which leads to Nur77 degradation. The Trim13-mediated ubiquitination of Nur77 was optimal in the presence of the E2 enzyme UbcH5. Importantly, in addition to Trim13-mediated ubiquitination, the stability of Nur77 was also regulated by casein kinase 2α (CK2α). Pharmacological inhibition of CK2 markedly increased Nur77 levels, whereas overexpression of CK2α, but not its inactive mutant, dramatically decreased Nur77 levels by promoting Nur77 ubiquitination. CK2α phosphorylated Ser154 in Nur77 and thereby regulated Nur77 protein levels by promoting its ubiquitin-mediated degradation. Importantly, we also show that degradation of Nur77 is involved in TNFα-mediated IL-6 production via CK2α and Trim13. Taken together, these results suggest that the sequential phosphorylation and ubiquitination of Nur77 controls its degradation, and provide a therapeutic approach for regulating Nur77 activity through the CK2α-Trim13 axis as a mechanism to control the inflammatory response.

Indexed as

Casein Kinase IICell LineDNA-Binding ProteinsHumansInterleukin-6Nuclear Receptor Subfamily 4, Group A, Member 1PhosphorylationProtein BindingProtein StabilityProteolysisSerineSignal TransductionTumor Necrosis Factor-alphaTumor Suppressor ProteinsUbiquitinationCasein Kinase IIDNA-Binding ProteinsIL6 protein, humanInterleukin-6NR4A1 protein, humanNuclear Receptor Subfamily 4, Group A, Member 1SerineTRIM13 protein, humanTumor Necrosis Factor-alphaTumor Suppressor Proteins

Identifiers

PMID30224829
PMCPMC6141542
OpenAlexW2891898291

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Registered trials

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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.