DRG1 is a potential oncogene in lung adenocarcinoma and promotes tumor progression via spindle checkpoint signaling regulation

Lü, Li; Lv, Yanrong; Ji, Dong; Hu, Shaohua; Peng, Ruiyun

doi:10.18632/oncotarget.11973

Cited by 20 publications

(33 citation statements)

References 34 publications

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“…that DRG1 was significantly up-regulated in OS cell lines when compared with normal human osteoblasts. Aberrantly expressed DRG1 has been observed in other types of cancers [10][11][12][13], but up-regulated DRG1 is not always associated with the worst types of cancer. For example, high Drg1 expression is more likely associated with a less aggressive and indolent colorectal cancer [13].…”

Section: Figure 3 Bioinformatics Analysis Revealed Drg1 Biological Fmentioning

confidence: 99%

“…Liu et al reported the interaction of DRG1 with kinetochore proteins (e.g. CENPN) and spindle assembly checkpoint proteins, such as Mad2 and BubR1 in lung adenocarcinomas [10]. Since these proteins are required for cell cycle and chromosomal segregation, it is possible that DRG1 also participates in the regulation of these functions.…”

Section: Figure 3 Bioinformatics Analysis Revealed Drg1 Biological Fmentioning

confidence: 99%

“…A growing number of studies have shown that abnormal expression of DRG1 is associated with occurrence and development of cancer. In lung adenocarcinoma, overexpressed DRG1 increased cell proliferation by regulating cell cycle proteins and enhanced resistance against paclitaxel (Taxol) [10].…”

Section: Introductionmentioning

confidence: 99%

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m6A-dependent up-regulation of DRG1 by METTL3 and ELAVL1 promotes growth, migration, and colony formation in osteosarcoma

2020

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Osteosarcoma (OS) is a malignant tumor commonly observed in children and adolescents. Developmentally regulated GTP-binding protein (DRG) 1 plays an important role in embryonic development; aberrantly expressed DRG1 has been associated with pathological processes in cancer. The present study aimed to explore the role of DRG1 in OS and the mechanisms underlying DRG1 overexpression in OS. Clinical studies were performed to evaluate Drg1 expression in OS tissues and to identify a correlation between Drg1 expression and the clinicopathological features in patients with OS. Drg1 was knocked down in OS cells to determine its effects on cell viability, cell cycle distribution, apoptosis, migration, invasion, and colony formation rate. METTL3 and ELAVL1 were also silenced to determine their effects on the levels of N6-methyladenosine (m6A), RNA stability, and Drg1 expression. Higher levels of Drg1 mRNA and protein were observed in OS tissues than those in paracancerous tissues. High expression of DRG1 was associated with large tumor size and advanced clinical stages in OS. Silencing of Drg1 resulted in decreased viability and inhibition of the migration and colony formation abilities of OS cells; it also resulted in cell cycle arrest in the G2/M stage and induced apoptosis. Knockdown of METTL3 led to decreased m6A and Drg1 mRNA levels. ELAVL1 knockdown impaired the stability of DRG1 mRNA, thereby reducing both the mRNA and protein levels of DRG1. In all, DRG1 exerted tumorigenic effects in OS, and the up-regulation of DRG1 in OS was induced by METTL3 and ELAVL1 in an m6A-dependent manner.

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Section: Figure 3 Bioinformatics Analysis Revealed Drg1 Biological Fmentioning

confidence: 99%

Section: Figure 3 Bioinformatics Analysis Revealed Drg1 Biological Fmentioning

confidence: 99%

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m6A-dependent up-regulation of DRG1 by METTL3 and ELAVL1 promotes growth, migration, and colony formation in osteosarcoma

2020

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“…IRS4 plays a tumor-promoting role in NSCLC (Hoxhaj, Dissanayake, & MacKintosh, 2013;Weischenfeldt et al, 2017). Overexpression of DRG1 leads to chromosome missegregation and promotes tumor progression in NSCLC (Lu, Lv, Dong, Hu, & Peng, 2016). Ten genes are uniquely identified by the proposed method, and the rest three (PSMD10, CMTX5, and LOC158602) are also identified by other methods.…”

Section: Lusc Datamentioning

confidence: 97%

“…DRG1 plays important roles in regulating cell growth. Overexpression of DRG1 leads to chromosome missegregation and promotes tumor progression in NSCLC (Lu, Lv, Dong, Hu, & Peng, 2016). GSR (glutathione reductase) is one of the enzymes in the glutathione (GSH) metabolism system, which is a major redox regulatory systems in mammals that support increased tumor growth (Tobe et al, 2015).…”

Section: Lusc Datamentioning

confidence: 99%

Robust network‐based regularization and variable selection for high‐dimensional genomic data in cancer prognosis

Ren

et al. 2019

Genetic Epidemiology

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In cancer genomic studies, an important objective is to identify prognostic markers associated with patients' survival. Network‐based regularization has achieved success in variable selections for high‐dimensional cancer genomic data, because of its ability to incorporate the correlations among genomic features. However, as survival time data usually follow skewed distributions, and are contaminated by outliers, network‐constrained regularization that does not take the robustness into account leads to false identifications of network structure and biased estimation of patients' survival. In this study, we develop a novel robust network‐based variable selection method under the accelerated failure time model. Extensive simulation studies show the advantage of the proposed method over the alternative methods. Two case studies of lung cancer datasets with high‐dimensional gene expression measurements demonstrate that the proposed approach has identified markers with important implications.

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Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7

Bilgin,

Tumber,

Dhingra

et al. 2024

Protein Science

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Jumonji‐C (JmjC) domain‐containing protein 7 (JMJD7) is a human Fe(II) and 2‐oxoglutarate dependent oxygenase that catalyzes stereospecific C3‐hydroxylation of lysyl‐residues in developmentally regulated GTP binding proteins 1 and 2 (DRG1/2). We report studies exploring a diverse set of lysine derivatives incorporated into the DRG1 peptides as potential human JMJD7 substrates and inhibitors. The results indicate that human JMJD7 has a relatively narrow substrate scope beyond lysine compared to some other JmjC hydroxylases and lysine‐modifying enzymes. The geometrically constrained (E)‐dehydrolysine is an efficient alternative to lysine for JMJD7‐catalyzed C3‐hydroxylation. γ‐Thialysine and γ‐azalysine undergo C3‐hydroxylation, followed by degradation to formylglycine. JMJD7 also catalyzes the S‐oxidation of DRG1‐derived peptides possessing methionine and homomethionine residues in place of lysine. Inhibition assays show that DRG1 variants possessing cysteine/selenocysteine instead of the lysine residue efficiently inhibit JMJD7 via cross‐linking. The overall results inform on the substrate selectivity and inhibition of human JMJD7, which will help enable the rational design of selective small‐molecule and peptidomimetic inhibitors of JMJD7.

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DRG1 is a potential oncogene in lung adenocarcinoma and promotes tumor progression via spindle checkpoint signaling regulation

Cited by 20 publications

References 34 publications

m6A-dependent up-regulation of DRG1 by METTL3 and ELAVL1 promotes growth, migration, and colony formation in osteosarcoma

m6A-dependent up-regulation of DRG1 by METTL3 and ELAVL1 promotes growth, migration, and colony formation in osteosarcoma

Robust network‐based regularization and variable selection for high‐dimensional genomic data in cancer prognosis

Substrate selectivity and inhibition of the human lysyl hydroxylase JMJD7

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