Evidence map›Paper›PMID 32327643›Full record

ArticleSignal transduction and targeted therapy2020

The CRL3

Lihui Li, Wenjuan Zhang, Yue Liu, Xiaojun Liu, Lili Cai, Jihui Kang, Yunjing Zhang, Wenlian Chen, Changsheng Dong, Yanmei Zhang and 3 more

Open access · goldAbstract read
In one paragraph

Article in Signal transduction and targeted therapy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  3. Advances of E3 ligases in lung cancer.Biochemistry and biophysics reports · 2024
    Review
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  9. Review
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  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. KCells · 2020
    Article
  17. 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

13 authors at 5 institutions in 2 countries.

Lihui Li *Cancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China. dm-li@163.com.
Wenjuan Zhang *Cancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Yue LiuDepartment of Laboratory Medicine, Huadong Hospital, Affiliated to Fudan University, Shanghai, China.
Xiaojun LiuCancer Institute, Fudan University Shanghai Cancer Center, Fudan University, Shanghai, China.
Lili CaiCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Jihui KangCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Yunjing ZhangCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Wenlian ChenCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Changsheng DongCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Yanmei ZhangDepartment of Laboratory Medicine, Huadong Hospital, Affiliated to Fudan University, Shanghai, China.
Mingsong WangXinhua Hospital, Shanghai Jiaotong University, Shanghai, China.
Wenyi WeiDepartment of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0003-0512-3811
Lijun JiaCancer Institute, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China. ljjia@shutcm.edu.cn.
Shanghai University of Traditional Chinese Medicine · CNFudan University · CNFudan University Shanghai Cancer Center · CNBeth Israel Deaconess Medical Center · USXinHua Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tumor necrosis factor alpha-induced protein 1 (TNFAIP1) modulates a plethora of important biological processes, including tumorigenesis and cancer cell migration. However, the regulatory mechanism of TNFAIP1 degradation remains largely elusive. In the present study, with a label-free quantitative proteomic approach, TNFAIP1 was identified as a novel ubiquitin target of the Cullin-RING E3 ubiquitin ligase (CRL) complex. More importantly, Cul3-ROC1 (CRL3), a subfamily of CRLs, was identified to specifically interact with TNFAIP1 and promote its polyubiquitination and degradation. Mechanistically, BTBD9, a specific adaptor component of CRL3 complex, was further defined to bind and promote the ubiquitination and degradation of TNFAIP1 in cells. As such, downregulation of BTBD9 promoted lung cancer cell migration by upregulating the expression of TNFAIP1, whereas TNFAIP1 deletion abrogated this effect. Finally, bioinformatics and clinical sample analyses revealed that BTBD9 was downregulated while TNFAIP1 was overexpressed in human lung cancer, which was associated with poor overall survival of patients. Taken together, these findings reveal a previously unrecognized mechanism by which the CRL3

Indexed as

Adaptor Proteins, Signal TransducingCarcinogenesisCell MovementCell ProliferationGene Expression Regulation, NeoplasticHep G2 CellsHumansMultiprotein ComplexesNeoplasmsNerve Tissue ProteinsProteolysisProteomicsUbiquitinationUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingBTBD9 protein, humanCULL-RING ligase, humanMultiprotein ComplexesNerve Tissue ProteinsTNFAIP1 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID32327643
PMCPMC7181851
OpenAlexW3020245587

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.