Evidence map›Paper›PMID 42265299›Full record

ArticleScientific reports2026

Ubiquitination of Smad2 by Smurf1 inhibits endothelial-to-mesenchymal transition in human coronary artery endothelial cells.

Panpan Liu, Mingyang Zhang, Shuhui Wang, Zhiheng Liu, Nana Wang, Zhiyuan Liu, Yiyi Shen, Jiaying Zhang, Jing Li, Ying Liu and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Panpan Liu *Institute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Mingyang Zhang *Institute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Shuhui Wang *Institute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Zhiheng LiuInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Nana WangInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Zhiyuan LiuInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Yiyi ShenDepartment of Cardiology, Children's Hospital of Soochow University, Suzhou, 215025, China.
Jiaying ZhangInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Jing LiInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Ying LiuInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China.
Haitao LvInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China. haitaosz@163.com.
Guanghui QianInstitute of Pediatric Research, Children's Hospital of Soochow University, Zhongnan Street, Suzhou, 215025, Jiangsu, China. ghqian@suda.edu.cn.

Funding

National Natural Science Foundation of China 82171797
6 · The paper itself

Abstract

Smad2 is a well-established regulator involved in tissue development and in the pathogenesis of endothelial-to-mesenchymal transition (EndMT) mediated by TGF-β signaling. However, the mechanism underlying the regulation of SMAD2 in human coronary artery endothelial cells (HCAECs), particularly the identity of the responsible E3 ubiquitin ligase and its role during EndMT remain unclear. In this study, we identified Smad ubiquitination regulatory factor 1 (Smurf1) as a negative regulator of Smad2 protein levels in HCAECs and demonstrated that the E3 ligase activity of Smurf1 is essential for this function. Mechanistically, Smurf1 interacts with Smad2, promoting its ubiquitination, and subsequent proteasomal degradation. Specifically, Smurf1 catalyzes K48-linked polyubiquitination of Smad2 at lysine residues K156, K383 and K420. Functionally, Smad2 was found to promote EndMT in HCAECs, an effect that was partially attenuated either by co-expression of Smurf1 or by mutation of Smad2 at lysine 420 (Smad2-K420R), which replaces lysine with arginine. Taken together, our findings identify, for the first time, specific lysine residues on Smad2 targeted by Smurf1 for K48-linked ubiquitination and highlight their crucial regulatory role in modulating EndMT in HCAECs.

Indexed as

Coronary VesselsEndothelial CellsEndothelial-Mesenchymal TransitionSmad2 ProteinUbiquitinationUbiquitin-Protein LigasesHumansLysineSignal TransductionLysineSmad2 ProteinSMAD2 protein, humanSMURF1 protein, humanUbiquitin-Protein LigasesEndMTHCAECSmad2Smurf1Ubiquitin

Identifiers

PMID42265299
PMCPMC13493842

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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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 Socratic graph.