Evidence map›Paper›PMID 24336050›Full record

ArticleCell death and differentiation2014

Suppression of PPARγ through MKRN1-mediated ubiquitination and degradation prevents adipocyte differentiation.

J-H Kim, K W Park, E-W Lee, W-S Jang, J Seo, S Shin, K-A Hwang, J Song

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

68 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Caspase-6 Controls Lipid and Energy Metabolism in Diet-Induced Obesity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Article
  7. Mixtures ofToxics · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Regulation of PPARγ2 Stability and Activity by SHP-1.Molecular and cellular biology · 2024
    Article
  16. Article
  17. Article
  18. Roles of Protein Post-Translational Modifications During Adipocyte Senescence.International journal of biological sciences · 2023
    Review
  19. Review
  20. Article

8 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

8 authors at 2 institutions in 1 country.

J-H KimDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
K W ParkDepartment of Food Science and Biotechnology, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi-do 440-746, Republic of Korea.
E-W LeeDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
W-S JangDepartment of Food Science and Biotechnology, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon, Gyeonggi-do 440-746, Republic of Korea.
J SeoDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
S ShinDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
K-A HwangDepartment of Agrofood Resources, National Academy of Agricultural Science, RDA, Suwon 441-853, Republic of Korea.
J SongDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.
Yonsei University · KRNational Academy of Agricultural Science · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The central regulator of adipogenesis, PPARγ, is a nuclear receptor that is linked to obesity and metabolic diseases. Here we report that MKRN1 is an E3 ligase of PPARγ that induces its ubiquitination, followed by proteasome-dependent degradation. Furthermore, we identified two lysine sites at 184 and 185 that appear to be targeted for ubiquitination by MKRN1. Stable overexpression of MKRN1 reduced PPARγ protein levels and suppressed adipocyte differentiation in 3T3-L1 and C3H10T1/2 cells. In contrast, MKRN1 depletion stimulated adipocyte differentiation in these cells. Finally, MKRN1 knockout MEFs showed an increased capacity for adipocyte differentiation compared with wild-type MEFs, with a concomitant increase of PPARγ and adipogenic markers. Together, these data indicate that MKRN1 is an elusive PPARγ E3 ligase that targets PPARγ for proteasomal degradation by ubiquitin-dependent pathways, and further depict MKRN1 as a novel target for diseases involving PPARγ.

Indexed as

3T3-L1 CellsAdipocytesAdipogenesisAnimalsCell DifferentiationCells, CulturedHEK293 CellsHumansLysineMiceMice, Inbred C57BLNerve Tissue ProteinsPPAR gammaRibonucleoproteinsRNA InterferenceRNA, MessengerLysineMakorin ring finger protein 1Nerve Tissue ProteinsPPAR gammaRibonucleoproteinsRNA, MessengerRNA, Small Interfering

Identifiers

PMID24336050
PMCPMC3950322
OpenAlexW1998290880

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.