Evidence map›Paper›PMID 36631457›Full record

ArticleCell death & disease2023

FRMD3 inhibits the growth and metastasis of breast cancer through the ubiquitination-mediated degradation of vimentin and subsequent impairment of focal adhesion.

Wenjun Shao, Jiawei Li, Qianling Piao, Xinlei Yao, Mingyue Li, Shuyue Wang, Zhenbo Song, Ying Sun, Lihua Zheng, Guannan Wang and 5 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death & disease, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

23 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Clinicopathological Characteristics of Upper Tract Urothelial Cancer With Loss of Immunohistochemical Expression of Mismatch Repair Proteins.International journal of urology : official journal of the Japanese Urological Association · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

15 authors at 1 institution in 1 country.

Wenjun ShaoNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.
Jiawei LiNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.
Qianling PiaoNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.
Xinlei YaoNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.
Mingyue LiNMPA Key Laboratory for Quality of Cell and Gene Therapy Medicinal Products, Northeast Normal University, Changchun, 130024, China.
Shuyue WangNMPA Key Laboratory for Quality of Cell and Gene Therapy Medicinal Products, Northeast Normal University, Changchun, 130024, China.
Zhenbo SongNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.
Ying SunNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.
Lihua ZhengNMPA Key Laboratory for Quality of Cell and Gene Therapy Medicinal Products, Northeast Normal University, Changchun, 130024, China.
Guannan WangNMPA Key Laboratory for Quality of Cell and Gene Therapy Medicinal Products, Northeast Normal University, Changchun, 130024, China.
Lei LiuNMPA Key Laboratory for Quality of Cell and Gene Therapy Medicinal Products, Northeast Normal University, Changchun, 130024, China.
Chunlei YuNMPA Key Laboratory for Quality of Cell and Gene Therapy Medicinal Products, Northeast Normal University, Changchun, 130024, China.
Yanxin HuangNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.
Yongli BaoNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China.ORCID 0000-0002-5972-1983
Luguo SunNational Engineering Laboratory for Druggable Gene and Protein Screening, Northeast Normal University, Changchun, 130024, China. sunlg388@nenu.edu.cn.ORCID 0000-0002-0895-8120
Northeast Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recurrence and metastasis are the main causes of breast cancer (BRCA)-related death and remain a challenge for treatment. In-depth research on the molecular mechanisms underlying BRCA progression has been an important basis for developing precise biomarkers and therapy targets for early prediction and treatment of progressed BRCA. Herein, we identified FERM domain-containing protein 3 (FRMD3) as a novel potent BRCA tumor suppressor which is significantly downregulated in BRCA clinical tissue and cell lines, and low FRMD3 expression has been closely associated with progressive BRCA and shortened survival time in BRCA patients. Overexpression and knockdown experiments have revealed that FRMD3 significantly inhibits BRCA cell proliferation, migration, and invasion in vitro and suppresses BRCA xenograft growth and metastasis in vivo as well. Mechanistically, FRMD3 can interact with vimentin and ubiquitin protein ligase E3A(UBE3A) to induce the polyubiquitin-mediated proteasomal degradation of vimentin, which subsequently downregulates focal adhesion complex proteins and pro-cancerous signaling activation, thereby resulting in cytoskeletal rearrangement and defects in cell morphology and focal adhesion. Further evidence has confirmed that FRMD3-mediated vimentin degradation accounts for the anti-proliferation and anti-metastasis effects of FRMD3 on BRCA. Moreover, the N-terminal ubiquitin-like domain of FRMD3 has been identified as responsible for FRMD3-vimentin interaction through binding the head domain of vimentin and the truncated FRMD3 with the deletion of ubiquitin-like domain almost completely loses the anti-BRCA effects. Taken together, our study indicates significant potential for the use of FRMD3 as a novel prognosis biomarker and a therapeutic target of BRCA and provides an additional mechanism underlying the degradation of vimentin and BRCA progression.

Indexed as

Breast NeoplasmsFocal AdhesionsTumor Suppressor ProteinsVimentinCell Line, TumorCell MovementCell ProliferationFemaleGene Expression Regulation, NeoplasticHumansUbiquitinUbiquitinationFRMD3 protein, humanTumor Suppressor ProteinsUbiquitinVimentin

Identifiers

PMID36631457
PMCPMC9834407
OpenAlexW4315568047

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.