Evidence map›Paper›PMID 31409387›Full record

ArticleJournal of experimental & clinical cancer research : CR2019

DTL promotes cancer progression by PDCD4 ubiquitin-dependent degradation.

Haoran Cui, Qin Wang, Zhenchuan Lei, Maoxiao Feng, Zhongxi Zhao, Yunshan Wang, Guangwei Wei

Open access · goldAbstract read
In one paragraph

Article in Journal of experimental & clinical cancer research : CR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.0field-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

66 citing papers in PubMed, 141 citations in OpenAlex.

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6 more citing papers are in PubMed but not listed here.

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

7 authors at 4 institutions in 1 country.

Haoran CuiDepartment of Cell Biology and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Jinan, Shandong, China.
Qin WangDepartment of Anesthesiology, Qilu Hospital, Shandong University, Jinan, Shandong, China.
Zhenchuan LeiCollege of Marine Life Sciences, Ocean University of China, Qingdao, Shandong, China.
Maoxiao FengDepartment of Cell Biology and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Jinan, Shandong, China.
Zhongxi ZhaoSchool of Pharmaceutical Sciences, Shandong University, No. 44 West Wenhua Road, Jinan, Shandong, China.
Yunshan WangDepartment of Clinical Laboratory, The Second Hospital of Shandong University, Jinan, Shandong, China. wangyunshan135@126.com.
Guangwei WeiDepartment of Cell Biology and Key Laboratory of Experimental Teratology, Ministry of Education, Shandong University School of Medicine, Jinan, Shandong, China. gwwei@yahoo.com.
Shandong University · CNOcean University of China · CNQilu Hospital of Shandong University · CNSecond Hospital of Shandong University · CN

Funding

National Key R&D Program of China 2017YFC1308600National Natural Science Foundation of China 81872148National Natural Science Foundation of China 81874040
6 · The paper itself

Abstract

backgroundUbiquitin E3 ligase CUL4A plays important oncogenic roles in the development of cancers. DTL, one of the CUL4-DDB1 associated factors (DCAFs), may involve in the process of cancer development. Programmed cell death 4 (PDCD4) is a tumor suppressor gene involved in cell apoptosis, transformation, invasion and tumor progression.

methodsAffinity-purification mass spectrometry was used to identify potential DTL interaction proteins. Co-immunoprecipitation (Co-IP) was performed to verify protein interaction between DTL and PDCD4. mRNA levels in cancer cells and tissues were detected by Quantitative real-time PCR. Lentivirus was used to establish stable overexpression and knocking down cell lines for DTL and PDCD4. Transwell and wound healing assays were used to determine migration ability of cancer cells. Matrigel assay was used to determine invasion ability of cancer cells. MTT and colony formation assays were used to evaluate proliferation of cancer cells.

resultsIn this study, programmed cell death 4 (PDCD4) was identified as a potential substrate of DTL. Co-IP and immunofluorescence assays further confirmed the interaction between DTL and PDCD4. Moreover, DTL overexpression decreased the protein level and accelerated the degradation rate of PDCD4. Through in vitro ubiquitination experiment, we proved that PDCD4 was degraded by DTL through ubiquitination. Clinically DTL was significantly up-regulated in cancer tissues than that in normal tissues. The survival curves showed that cancer patients with higher DTL expression owned lower survival rate. Functional experiments showed that DTL not only enhanced the proliferation and migration abilities of cancer cells, but also promoted the tumorigenesis in nude mice. Rescued experiment results demonstrated that silencing PDCD4 simultaneous with DTL recovered the phenotypes defect caused by DTL knocking down.

conclusionsOur results elucidated that DTL enhanced the motility and proliferation of cancer cells through degrading PDCD4 to promote the development of cancers.

Indexed as

AnimalsApoptosisApoptosis Regulatory ProteinsCell Line, TumorCell MovementCell ProliferationComputational BiologyDisease Models, AnimalHeterograftsHumansMiceNeoplasmsNuclear ProteinsProteasome Endopeptidase ComplexProteolysisRNA-Binding ProteinsApoptosis Regulatory ProteinsDTL protein, humanNuclear ProteinsPDCD4 protein, humanProteasome Endopeptidase ComplexRNA-Binding ProteinsUbiquitinsCancer developmentCUL4ADTLPDCD4

Identifiers

PMID31409387
PMCPMC6693180
OpenAlexW2967369839

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.