Evidence map›Paper›PMID 30323259›Full record

ArticleExperimental & molecular medicine2018

The E3 ubiquitin ligase TRIM25 regulates adipocyte differentiation via proteasome-mediated degradation of PPARγ.

Jae Min Lee, Sun Sil Choi, Yo Han Lee, Keon Woo Khim, Sora Yoon, Byung-Gyu Kim, Dougu Nam, Pann-Ghill Suh, Kyungjae Myung, Jang Hyun Choi

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

29 citing papers in PubMed, 33 citations in OpenAlex.

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  15. Article
  16. Regulation of PPARγ2 Stability and Activity by SHP-1.Molecular and cellular biology · 2024
    Article
  17. Article
  18. ISGylation of NF-κBp65 by SCFArteriosclerosis, thrombosis, and vascular biology · 2023
    Article
  19. Roles of Protein Post-Translational Modifications During Adipocyte Senescence.International journal of biological sciences · 2023
    Review
  20. Article
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

10 authors at 2 institutions in 1 country.

Jae Min LeeDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Sun Sil ChoiDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Yo Han LeeDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Keon Woo KhimDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Sora YoonDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Byung-Gyu KimCenter for Genomic Integrity (CGI), Institute for Basic Science (IBS), Department of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Dougu NamDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Pann-Ghill SuhDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Kyungjae MyungDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea.
Jang Hyun ChoiDepartment of Biological Sciences, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 689-798, Korea. janghchoi@unist.ac.kr.
Ulsan National Institute of Science and Technology · KRInstitute for Basic Science · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisome proliferator-activated receptor gamma (PPARγ) is a ligand-dependent transcription factor that regulates adipocyte differentiation and glucose homeostasis. The transcriptional activity of PPARγ is regulated not only by ligands but also by post-translational modifications (PTMs). In this study, we demonstrate that a novel E3 ligase of PPARγ, tripartite motif-containing 25 (TRIM25), directly induced the ubiquitination of PPARγ, leading to its proteasome-dependent degradation. During adipocyte differentiation, both TRIM25 mRNA and protein expression significantly decreased and negatively correlated with the expression of PPARγ. The stable expression of TRIM25 reduced PPARγ protein levels and suppressed adipocyte differentiation in 3T3-L1 cells. In contrast, the specific knockdown of TRIM25 increased PPARγ protein levels and stimulated adipocyte differentiation. Furthermore, TRIM25-knockout mouse embryonic fibroblasts (MEFs) exhibited an increased adipocyte differentiation capability compared with wild-type MEFs. Taken together, these data indicate that TRIM25 is a novel E3 ubiquitin ligase of PPARγ and that TRIM25 is a novel target for PPARγ-associated metabolic diseases.

Indexed as

Cell Differentiation3T3-L1 CellsAdipocytesAnimalsHEK293 CellsHumansMicePPAR gammaProteasome Endopeptidase ComplexProtein BindingProtein StabilityProteolysisTranscription FactorsTripartite Motif ProteinsUbiquitin-Protein LigasesPPAR gammaProteasome Endopeptidase ComplexTranscription FactorsTRIM25 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID30323259
PMCPMC6189217
OpenAlexW2897270085

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.