Evidence map›Paper›PMID 25091805›Full record

Trial reportJournal of biomedical science2014

A putative novel protein, DEPDC1B, is overexpressed in oral cancer patients, and enhanced anchorage-independent growth in oral cancer cells that is mediated by Rac1 and ERK.

Ying-Fang Su, Chi-Yen Liang, Chih-Yang Huang, Chih-Yu Peng, Claire Chiyu Chen, Ming-Cheng Lin, Rong-Kai Lin, Wei-Wen Lin, Ming-Yung Chou, Pao-Hsin Liao and 1 more

Open access · diamondAbstract readClinical Trial
In one paragraph

Trial report in Journal of biomedical science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 26% 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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Pooled it
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  4. Annals of translational medicine · 2023
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  8. Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022
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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

11 authors at 6 institutions in 2 countries.

Ying-Fang Su
Chi-Yen Liang
Chih-Yang Huang
Chih-Yu Peng
Claire Chiyu Chen
Ming-Cheng Lin
Rong-Kai Lin
Wei-Wen Lin
Ming-Yung Chou
Pao-Hsin Liao
Jaw-Ji Yang
China Medical University · TWAsia University · TWChia-Yi Christian Hospital · TWChung Shan Medical University · TWTaichung Veterans General Hospital · TWUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe DEP domain is a globular domain containing approximately 90 amino acids, which was first discovered in 3 proteins: Drosophila disheveled, Caenorhabditis elegans EGL-10, and mammalian Pleckstrin; hence the term, DEP. DEPDC1B is categorized as a potential Rho GTPase-activating protein. The function of the DEP domain in signal transduction pathways is not fully understood. The DEPDC1B protein exhibits the characteristic features of a signaling protein, and contains 2 conserved domains (DEP and RhoGAP) that are involved in Rho GTPase signaling. Small GTPases, such as Rac, CDC42, and Rho, regulate a multitude of cell events, including cell motility, growth, differentiation, cytoskeletal reorganization and cell cycle progression.

resultsIn this study, we found that it was a guanine nucleotide exchange factor and induced both cell migration in a cultured embryonic fibroblast cell line and cell invasion in cancer cell lines; moreover, it was observed to promote anchorage-independent growth in oral cancer cells. We also demonstrated that DEPDC1B plays a role in regulating Rac1 translocated onto cell membranes, suggesting that DEPDC1B exerts a biological function by regulating Rac1. We examined oral cancer tissue; 6 out of 7 oral cancer tissue test samples overexpressed DEPDC1B proteins, compared with normal adjacent tissue.

conclusionsDEPDC1B was a guanine nucleotide exchange factor and induced both cell migration in a cultured embryonic fibroblast cell line and cell invasion in cancer cell lines; moreover, it was observed to promote anchorage-independent growth in oral cancer cells. We also demonstrated that DEPDC1B exerts a biological function by regulating Rac1. We found that oral cancer samples overexpressed DEPDC1B proteins, compared with normal adjacent tissue. Suggest that DEPDC1B plays a role in the development of oral cancer. We revealed that proliferation was linked to a novel DEPDC1B-Rac1-ERK1/2 signaling axis in oral cancer cell lines.

Indexed as

Cell ProliferationGene Expression Regulation, NeoplasticMAP Kinase Signaling SystemCell Cycle ProteinsCell Line, TumorFemaleGTPase-Activating ProteinsHumansMaleMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mouth NeoplasmsNeoplasm ProteinsProtein Transportrac1 GTP-Binding ProteinCell Cycle ProteinsDEPDC1B protein, humanGTPase-Activating ProteinsMAPK1 protein, humanMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Neoplasm Proteinsrac1 GTP-Binding ProteinRAC1 protein, human

Identifiers

PMID25091805
PMCPMC4237807
OpenAlexW2136358702

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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 OpenQuestion graph.