Evidence map›Paper›PMID 35397617›Full record

ArticleCell death discovery2022

HECTD3 promotes gastric cancer progression by mediating the polyubiquitination of c-MYC.

Guanghui Zhang, Qingzong Zhu, Xiaomin Yan, Mingxin Ci, Erhu Zhao, Jianbing Hou, Sicheng Wan, Muhan Lü, Hongjuan Cui

Open access · goldAbstract read
In one paragraph

Article in Cell death discovery, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. RNF20 contributes to epigenetic immunosuppression through CDK9-dependent LSD1 stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. 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

9 authors at 2 institutions in 1 country.

Guanghui ZhangState Key Laboratory of Silkworm Genome Biology, Southwest University, 400716, Chongqing, China.
Qingzong ZhuState Key Laboratory of Silkworm Genome Biology, Southwest University, 400716, Chongqing, China.
Xiaomin YanChongqing iCELL Biotechnology Co Ltd, Chongqing, People's Republic of China.
Mingxin CiState Key Laboratory of Silkworm Genome Biology, Southwest University, 400716, Chongqing, China.
Erhu ZhaoState Key Laboratory of Silkworm Genome Biology, Southwest University, 400716, Chongqing, China.ORCID http://orcid.org/0000-0001-5606-5450
Jianbing HouState Key Laboratory of Silkworm Genome Biology, Southwest University, 400716, Chongqing, China.
Sicheng WanState Key Laboratory of Silkworm Genome Biology, Southwest University, 400716, Chongqing, China.
Muhan LüDepartment of Gastroenterology, The Affiliated Hospital of Southwest Medical University, 646000, Luzhou, China. lvmuhan@swmu.edu.cn.ORCID http://orcid.org/0000-0002-0527-3695
Hongjuan CuiState Key Laboratory of Silkworm Genome Biology, Southwest University, 400716, Chongqing, China. hongjuan.cui@gmail.com.ORCID http://orcid.org/0000-0003-1178-1570
Southwest University · CNSouthwest Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The E3 ubiquitin ligase HECTD3 is homologous with the E6 related protein carboxyl terminus, which plays a vital role in biological modification, including immunoreactivity, drug resistance and apoptosis. Current research indicates that HECTD3 promotes the malignant proliferation of multiple tumors and increases drug tolerance. Our study primarily explored the important function and effects of HECTD3 in gastric cancer. Here, we discovered that HECTD3 is abnormally activated in gastric cancer, and the clinical prognosis database suggested that HECTD3 was strongly expressed in gastric cancer. Depletion of HECTD3 restrained the proliferative and clone abilities of cells and induced the apoptosis of gastric cancer cells. Mechanistically, our findings revealed that interaction between HECTD3 and c-MYC, and that the DOC domain of HECTD3 interacted with the CP and bHLHZ domains of c-MYC. Furthermore, we discovered that HECTD3 mediates K29-linked polyubiquitination of c-MYC. Then, our research indicated that cysteine mutation at amino acid 823 (ubiquitinase active site) of HECTD3 reduces the polyubiquitination of c-MYC. Our experimental results reveal that HECTD3 facilitates the malignant proliferation of gastric cancer by mediating K29 site-linked polyubiquitination of c-MYC. HECTD3 might become a curative marker.

Identifiers

PMID35397617
PMCPMC8994759
OpenAlexW4223585714

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.