RETRACTED ARTICLE: High Expression of RIOK2 and NOB1 Predict Human Non-small Cell Lung Cancer Outcomes

K, Liu; Chen, Hong‐Lin; Wang, Shuo; Gu, Ming; Chen, Xinming; Zhang, Shuang-Long; Yu, Kang-Jun; You, Qingsheng

doi:10.1038/srep28666

Cited by 34 publications

(34 citation statements)

References 36 publications

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“…In line with the up‐regulation of RIOK2 in lung cancer 33 and of RIOK3 in glioma tissues, 9 the elevated expression of RIOK2 was revealed by both qRT‐PCR and immunohistochemical analyses in our glioma specimens, especially in high‐grade gliomas. In addition, RIOK1 was significantly up‐regulated in colorectal cancer and associated with an aggressive and poor survival 30 .…”

Section: Discussionsupporting

confidence: 70%

RIOK2 is negatively regulated by miR‐4744 and promotes glioma cell migration/invasion through epithelial‐mesenchymal transition

Song

Cheng

Jin

et al. 2020

J Cellular Molecular Medi

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RIOK2 is a member of RIO (right open reading frame) kinase family. Recent studies have revealed the involvement of RIO kinases in glioma cell growth and expansion. However, the role and mechanism of RIOK2 in glioma cell migration and invasion remain unclear. Wound healing assay, Transwell assay and real-time quantitative PCR (qRT-PCR) detection of matrix metalloproteinases (MMPs) were used to evaluate the migration/invasion of glioma cells. Western blot and qRT-PCR were employed to measure the expression of epithelial-mesenchymal transition (EMT) markers. Dual luciferase reporter assay was performed to determine the binding between RIOK2 and miR-4744. In addition, RIOK2 and miR-4744 levels were quantified by qRT-PCR and/ or immunohistochemistry in glioma tissues. Transfection of RIOK2 siRNAs significantly inhibited glioma cell migration and invasion and down-regulated the expression of MMPs (MMP2 and MMP9) and mesenchymal markers (N-cadherin, β-catenin, Twist1, fibronectin, ZEB-1) in glioma cells. Overexpression of RIOK2 showed the opposite effects. MiR-4744 directly bound to the 3'-untranslated region of RIOK2 and negatively regulated the expression of RIOK2. Up-regulation of miR-4744 inhibited the migration and invasion of glioma cells. Overexpression of RIOK2 could reverse the effects of miR-4744 up-regulation on the migration, invasion and EMT process in glioma cells. Moreover, RIOK2 was high, while miR-4744 was low in glioma tissues, and a negative correlation was found between them. These results suggest that RIOK2 is post-transcriptionally targeted by miR-4744, the low miR-4744 and high RIOK2 levels in glioma may contribute to tumour cell infiltration through promoting the EMT. K E Y W O R D S fibronectin, glioma, miR-4744, N-cadherin, RIOK2, β-catenin | 4495 SONG et al. S U PP O RTI N G I N FO R M ATI O N Additional supporting information may be found online in the Supporting Information section. How to cite this article: Song Y, Li C, Jin L, et al. RIOK2 is negatively regulated by miR-4744 and promotes glioma cell migration/invasion through epithelial-mesenchymal transition.

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Section: Discussionsupporting

confidence: 70%

RIOK2 is negatively regulated by miR‐4744 and promotes glioma cell migration/invasion through epithelial‐mesenchymal transition

Song

Cheng

Jin

et al. 2020

J Cellular Molecular Medi

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“…These DEGs suggest that PNO1 may participate in several pathways involved in cell-cycle progression and proliferation, including p53/p21 signaling. Activation of the well-known tumor suppressor p53 induces transcription of various genes, including the p21 gene, which can lead to cell-cycle arrest and apoptosis as well as inhibit cell proliferation (35)(36)(37)(38)(39). Various cellular insults can activate p53, including disruption of ribosome biogenesis (21,40,41).…”

Section: Discussionmentioning

confidence: 99%

EBF1-Mediated Upregulation of Ribosome Assembly Factor PNO1 Contributes to Cancer Progression by Negatively Regulating the p53 Signaling Pathway

et al. 2019

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The RNA-binding protein PNO1 is critical for ribosome biogenesis, but its potential role in cancer remains unknown. In this study, online data mining, cDNA, and tissue microarrays indicated that PNO1 expression was higher in colorectal cancer tissue than in noncancerous tissue, and its overexpression was associated with worse patient survival. Gain-offunction and loss-of-function studies demonstrated that PNO1 knockdown suppressed growth of colorectal cancer cells in vitro and in vivo, while PNO1 overexpression promoted colorectal cancer cell proliferation in vitro. In colorectal cancer cells expressing wild-type p53, PNO1 knockdown enhanced expression of p53 and its downstream gene p21, and reduced cell viability; these effects were prevented by p53 knockout and attenuated by the p53 inhibitor PFT-a. Moreover, PNO1 knockdown in HCT116 cells decreased levels of 18S rRNA, of 40S and 60S ribosomal subunits, and of the 80S ribosome. It also reduced global protein synthesis, increasing nuclear stress and inhibiting MDM2-mediated ubiquitination and p53 degradation. Overexpressing EBF1 suppressed PNO1 promoter activity and decreased PNO1 mRNA and protein, inhibiting cell proliferation and inducing cell apoptosis through the p53/p21 pathway. In colorectal cancer tissues, the expression of EBF1 correlated inversely with PNO1. Data mining of online breast and lung cancer databases showed increased PNO1 expression and association with poor patient survival; PNO1 knockdown reduced cell viability of cultured breast and lung cancer cells. Taken together, these findings indicate that PNO1 is overexpressed in colorectal cancer and correlates with poor patient survival, and that PNO1 exerts oncogenic effects, at least, in part, by altering ribosome biogenesis.Significance: This study identifies the ribosome assembly factor PNO1 as a potential oncogene involved in tumor growth and progression of colorectal cancer.

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“…Différentes équipes ont observé une surexpression de plusieurs facteurs impliqués dans la synthèse des ribosomes en corrélation avec la sévérité de certains cancers. Parmi ces facteurs, on retrouve la protéine GPATCH2 (G-patch domain-containing protein 2) qui régule l'activité de l'hélicase Prp43 (pre-mRNA-splicing factor ATP-dependent RNA helicase), le facteur d'assemblage hCINAP (human coilin-interacting nuclear ATPase protein), l'endonucléase Nob1 (NIN1/PSMD8 binding protein 1 homolog) et la kinase RIOK2 (RIO kinase 2)[13][14][15]. L'ensemble de ces observations ont engendré différentes hypothèses sur l'existence de liens directs entre synthèse des ribosomes et progression tumorale[16].…”

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La synthèse des ribosomes, au cœur du contrôle de la prolifération cellulaire

Madru¹,

Leulliot²,

Lebaron³

2017

Med Sci (Paris)

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Ribosomes are central to gene expression. Their assembly is a complex and an energy consuming process. Many controls exist to make it possible a fine-tuning of ribosome production adapted to cell needs. In this review, we describe recent advances in the characterisation of the links occurring between ribosome synthesis and cell proliferation control. Defects in ribosome biogenesis directly impede cellular cycle and slow-down proliferation. Among the different factors involved, we could define the 5S particle, a ribosome sub-complex, as a key-regulator of p53 and other tumour suppressors such as pRB. This cross-talk between ribosome neogenesis defects and proliferation and cellular cycle also involves other cell cycle controls such as p14, SRSF1 or PRAS40 pathways. These data place ribosome synthesis at the heart of cell proliferation and offer new therapeutic strategies against cancer.

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RETRACTED ARTICLE: High Expression of RIOK2 and NOB1 Predict Human Non-small Cell Lung Cancer Outcomes

Cited by 34 publications

References 36 publications

RIOK2 is negatively regulated by miR‐4744 and promotes glioma cell migration/invasion through epithelial‐mesenchymal transition

RIOK2 is negatively regulated by miR‐4744 and promotes glioma cell migration/invasion through epithelial‐mesenchymal transition

EBF1-Mediated Upregulation of Ribosome Assembly Factor PNO1 Contributes to Cancer Progression by Negatively Regulating the p53 Signaling Pathway

La synthèse des ribosomes, au cœur du contrôle de la prolifération cellulaire

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