Evidence map›Paper›PMID 37770719›Full record

ArticleNature structural & molecular biology2023

Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane.

Si Hoon Park, Juhyun Han, Byung-Cheon Jeong, Ju Han Song, Se Hwan Jang, Hyeongseop Jeong, Bong Heon Kim, Young-Gyu Ko, Zee-Yong Park, Kyung Eun Lee and 2 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity.International journal of molecular sciences · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 3 countries.

Si Hoon ParkDepartment of Life Sciences, Korea University, Seoul, South Korea.ORCID 0000-0003-3518-7808
Juhyun HanDepartment of Life Sciences, Korea University, Seoul, South Korea.
Byung-Cheon JeongDepartment of Life Sciences, Korea University, Seoul, South Korea.
Ju Han SongDepartment of Life Sciences, Korea University, Seoul, South Korea.
Se Hwan JangSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, South Korea.
Hyeongseop JeongCenter for Electron Microscopy Research, Korea Basic Science Institute, Cheongju-si, South Korea.ORCID 0000-0003-0095-3402
Bong Heon KimDepartment of Life Sciences, Korea University, Seoul, South Korea.
Young-Gyu KoDepartment of Life Sciences, Korea University, Seoul, South Korea.ORCID 0000-0002-0969-2598
Zee-Yong ParkSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, South Korea.
Kyung Eun LeeAdvanced Analysis Center, Korea Institute of Science and Technology, Seoul, South Korea.
Jaekyung HyunSchool of Pharmacy, Sungkyunkwan University, Suwon, South Korea.ORCID 0000-0003-2914-537X
Hyun Kyu SongDepartment of Life Sciences, Korea University, Seoul, South Korea. hksong@korea.ac.kr.ORCID 0000-0001-5684-4059
Korea University · KRGwangju Institute of Science and Technology · KRChonnam National University · KRKorea Basic Science Institute · KRKorea Institute of Science and Technology · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Defects in plasma membrane repair can lead to muscle and heart diseases in humans. Tripartite motif-containing protein (TRIM)72 (mitsugumin 53; MG53) has been determined to rapidly nucleate vesicles at the site of membrane damage, but the underlying molecular mechanisms remain poorly understood. Here we present the structure of Mus musculus TRIM72, a complete model of a TRIM E3 ubiquitin ligase. We demonstrated that the interaction between TRIM72 and phosphatidylserine-enriched membranes is necessary for its oligomeric assembly and ubiquitination activity. Using cryogenic electron tomography and subtomogram averaging, we elucidated a higher-order model of TRIM72 assembly on the phospholipid bilayer. Combining structural and biochemical techniques, we developed a working molecular model of TRIM72, providing insights into the regulation of RING-type E3 ligases through the cooperation of multiple domains in higher-order assemblies. Our findings establish a fundamental basis for the study of TRIM E3 ligases and have therapeutic implications for diseases associated with membrane repair.

Indexed as

Heart DiseasesUbiquitin-Protein LigasesAnimalsHumansMembrane ProteinsMiceModels, MolecularTripartite Motif ProteinsUbiquitinationMembrane ProteinsMG53 protein, mouseTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID37770719
PMCPMC10643145
OpenAlexW4387130457

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.