CNBP acts as a key transcriptional regulator of sustained expression of interleukin-6

Lee, Eun‐Hye; Lee, Taeyun A.; Kim, Ji Hyun; Park, Areum; Si, Euna; Kang, Su-Jin; Choi, Hyun Jin; Choi, Junhee; Huh, Hyunbin D.; Lee, Ji Eun; Lee, Sungwook; Park, Boyoun

doi:10.1093/nar/gkx071

Cited by 39 publications

(63 citation statements)

References 66 publications

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“…Because EGF triggers PKC activation, we further explored whether PKC phosphorylated CNBP in response to EGF. As previously noted, in vitro kinase assay showed that PKC phosphorylated CNBP as well as the NF‐κB subunit p65 (Figure S2). To determine whether EGF‐stimulated PKC induced CNBP nuclear translocation, we measured the amount of CNBP in the cytosolic and nuclear fractions from TC‐1 cells stimulated with EGF after pretreatment with the PKC inhibitor BIM‐I.…”

Section: Resultssupporting

confidence: 79%

“…We previously identified the specific CNBP‐binding motif sequence of CTGAAAAt(a), which is present in the promotors of its target inflammatory genes . Interestingly, the promoter regions of tumor‐related genes , such as mmp‐2 , kras , mmp‐14 , and e2f2 also contained a very similar motif alignment essential for CNBP binding (Figure A and Doc S2).…”

Section: Resultsmentioning

confidence: 94%

“…These findings led us to ask why there was a difference in the binding ability of CNBP between mmp‐2 / mmp‐14 / e2f2 and kras , despite their promoters all possessing the same CNBP‐binding core sequences (GAAAA) E).…”

Section: Resultsmentioning

confidence: 99%

“…It is broadly known that posttranslational modifications, including phosphorylation, ubiquitination, and dimerization, regulate the nuclear translocation of transcription factors. Our previous study showed that threonine (Thr) residues positioned at 173 and 177 of CNBP were indispensable for its phosphorylation and dimerization in response to lipopolysaccharide (LPS) exposure, leading to nuclear translocation . Therefore, we speculated that EGF would induce CNBP phosphorylation at Thr residues 173 and 177; however, neither Thr residue was involved in EGF‐mediated mmp‐2 expression, CNBP phosphorylation, and its dimerization (Figure S2).…”

Section: Resultsmentioning

confidence: 99%

“…CNBP has been implicated in diverse biological processes, acting as a nucleic acid chaperone and transcription factor. Several studies have shown that CNBP regulates the expression of macrophage colony‐stimulating factor ( csf1 ), c‐myc proto‐oncogene, Wnt signaling pathway components, and proinflammatory cytokines . In addition, CNBP is involved in embryonic forebrain development and various human diseases, including myotonic dystrophy type 2 (DM2) and sporadic inclusion body myositis (sIBM) .…”

Section: Introductionmentioning

confidence: 99%

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CNBP controls tumor cell biology by regulating tumor‐promoting gene expression

Lee

Yoo

et al. 2019

Molecular Carcinogenesis

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Cellular nucleic acid-binding protein (CNBP) is associated with cell proliferation, and its expression is elevated in human tumors, but the molecular mechanisms of CNBP in tumor cell biology have not been fully elucidated. In this study, we report that CNBP is a transcription factor essential for regulating matrix metalloproteinases mmp-2, mmp-14, and transcription factor e2f2 gene expression by binding to their promoter regions via a sequence-specific manner. Importantly, epidermal growth factor stimulation is required to induce CNBP phosphorylation and nuclear transport, thereby promoting the expression of mmp-2, mmp-14, and e2f2 genes. As a consequence, loss of cnbp attenuates the ability of tumor cell growth, invasion, and migration.Conversely, overexpression of cnbp is associated with tumor cell biology. Collectively, our findings reveal CNBP as a key transcriptional regulator of tumor-promoting target genes to control tumor cell biology. K E Y W O R D Scellular nucleic acid-binding protein, extracellular matrix, matrix metalloproteinase, transcription factor, tumor

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Section: Resultssupporting

confidence: 79%

Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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CNBP controls tumor cell biology by regulating tumor‐promoting gene expression

Lee

Yoo

et al. 2019

Molecular Carcinogenesis

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Unconventional RNA‐binding proteins: an uncharted zone in RNA biology

Albihlal

Gerber

2018

FEBS Letters

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The RNA-binding proteins play essential roles in the post-transcriptional regulation of gene expression. While hundreds of RNA-binding proteins can be predicted computationally, the recent introduction of proteome-wide approaches has dramatically expanded the repertoire of proteins interacting with RNA. Besides canonical RNA-binding proteins that contain characteristic RNA-binding domains, many proteins that lack such domains but have other well-characterized cellular functions were identified; including metabolic enzymes, heat shock proteins, kinases, as well as transcription factors and chromatin-associated proteins. In the context of these recently published RNA-protein interactome datasets obtained from yeast, nematodes, flies, plants and mammalian cells, we discuss examples for seemingly evolutionary conserved 'unconventional' RNA-binding proteins that act in central carbon metabolism, stress response or regulation of transcription.

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OSBPL10‐CNBP axis mediates hypoxia‐induced pancreatic cancer development

Huang,

Zhang,

Fan

et al. 2024

BioFactors

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Pancreatic ductal adenocarcinoma (PDAC) is one of malignancies with worst outcomes among digestive system tumors. Identification of novel biomarkers is of great significance for treatment researches and prognosis prediction of pancreatic cancer patients. Due to OSBPL10 known involvement in oncogenic activity in other tumors, we elucidated the mechanism underlying its contribution to pancreatic cancer progression. We employed data from the Gene Expression Omnibus database to detect the expression of OSBPL10 in normal and pancreatic cancer tissues. A series of assays were conducted to assess the impact of OSBPL10 on the proliferation and metastatic capacities of pancreatic cancer cells and the influence of OSBPL10 on macrophages were evaluated by Flow cytometry. In addition, Co‐immunoprecipitation, mass spectrometry, and western blot assays were utilized to investigate the potential mechanisms of OSBPL10 activity. From our study, OSBPL10 is revealed to be upregulated in pancreatic cancer, with poor prognosis. The overexpression promotes malignant behaviors of pancreatic cancer cells and has an impact on tumor immune microenvironment by stimulating the transformation M1 macrophages into M2 macrophages. Mechanistically, hypoxia induces the expression of OSBPL10 through interaction between hypoxia‐inducible factor 1‐α and the promoter region of OSBPL10. Additionally, OSBPL10 directly bound to CNBP, mediating CNBP expression and ultimately regulating the proliferation and metastasis capacity of pancreatic cancer cells, as well as influencing macrophage polarization. The research emphasized the oncogenic role of OSBPL10 in pancreatic cancer, uncovering key mechanisms involving hypoxia, HIF‐1α, and CNBP. The finding suggests that OSBPL10 is a novel biomarker in pancreatic cancer, making it a potential therapeutic target for intervention in this malignancy.

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CNBP acts as a key transcriptional regulator of sustained expression of interleukin-6

Cited by 39 publications

References 66 publications

CNBP controls tumor cell biology by regulating tumor‐promoting gene expression

CNBP controls tumor cell biology by regulating tumor‐promoting gene expression

Unconventional RNA‐binding proteins: an uncharted zone in RNA biology

OSBPL10‐CNBP axis mediates hypoxia‐induced pancreatic cancer development

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