Direct repression of the human IRF-3 promoter by E2F1

Xu, Hua‐Guo; Ren, Wei; Zou, Li; Wang, Yi; Jin, Rui; Zhou, Guoping

doi:10.1007/s00251-010-0505-5

Cited by 17 publications

(17 citation statements)

References 19 publications

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“…For these E2F1 binding sites, we used TTTSSCGC as a consensus sequence (Xu et al, 2011;Zou et al, 2012), where S represents C or G. Because of the E2F1 activity in tumorigenesis (Tsantoulis et al, 2005;Chen et al, 2009;Lee et al, 2010), we determined NELL2 expression in various breast (MCF7, MDA-MB231, and MDA-MB435) and bladder (UC5, EJ, 5637, and T24) cancer cell lines. The 5637 and MDA-MB231 cells showed more invasive activity than UC5 and MCF7 cancer cells by an invasion assay with Boyden chambers (Materials and Methods section).…”

Section: Resultsmentioning

confidence: 99%

Retracted: The E2F1 Oncogene Transcriptionally Regulates NELL2 in Cancer Cells

Kim

Roh

Lee

et al. 2013

DNA and Cell Biology

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NELL2 was first identified as a mammalian homolog of the chicken NEL protein. It was expressed in neurons and has been suggested to play a role in cell survival. However, no clear evidence has yet been available for functions of NELL2. In this study, we found two E2F1 binding sites located in the NELL2 promoter region. We examined the expression of NELL2 and E2F1 in human breast cancer cells (MDA-MB231, MCF7) and bladder cancer cells (5637, UC5). In MDA-MB231 and 5637, the expression levels of NELL2 and E2F1 were higher. To examine the interaction between E2F1 and NELL2, the binding activity was checked by a promoter assay and chromatin immunoprecipitation. From the results, we suggest that NELL2 is a novel target gene of E2F1, which is a key regulator of cell proliferation. We reveal that expression of NELL2 is regulated by E2F1, specifically, mRNA and protein levels of NELL2 are elevated upon activation of exogenous E2F1. Moreover, cells overexpressing NELL2 increased their invasive ability and an enhancement of the effect was observed when NELL2 and E2F1 were coexpressed in MDA-MB231 cells. Therefore, we suggest a novel activity for NELL2 in cancer progression through the regulation of E2F1.

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Section: Resultsmentioning

confidence: 99%

Retracted: The E2F1 Oncogene Transcriptionally Regulates NELL2 in Cancer Cells

Kim

Roh

Lee

et al. 2013

DNA and Cell Biology

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“…Sequence alignment between the consensus E2F binding site TTT (C/G)(C/G)CGC (59) and the predicted E2F binding sites shows very high identity with a threshold score of 85%. The identification of the E2F consensus binding site in the TLR2 and TLR4 promoters suggests that members of the E2F family may regulate TLR transcriptional expression as it has previously been described for other transcription factors such as IFN regulatory factor-3 (60).…”

Section: Discussionmentioning

confidence: 62%

The Tumor Suppressor ARF Regulates Innate Immune Responses in Mice

Través

López-Fontal

Luque

et al. 2011

The Journal of Immunology

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The innate immune system is the first line of defense against invading organisms, and TLRs are the main sensors of microbial components, initiating signaling pathways that induce the production of proinflammatory cytokines and type I IFNs. An antiviral action for the tumor suppressor alternative reading frame (ARF) has been reported; however, the precise role of ARF in innate immunity is unknown. In this study, we show that ARF plays an important role in regulation of inflammatory responses. In peritoneal macrophages and bone marrow-derived macrophages from ARF-deficient animals, the induction of proinflammatory cytokines and chemokines by TLR ligands was severely impaired. The altered responses of ARF−/− cells to TLR ligands result from aberrant activation of intracellular signaling molecules including MAPKs, IκBα degradation, and NF-κB activation. Additionally, animals lacking ARF were resistant to LPS-induced endotoxic shock. This impaired activation of inflammation in ARF−/− mice was not restricted to TLRs, as it was also shown in response to non-TLR signaling pathways. Thus, ARF−/− mice were also unable to trigger a proper inflammatory response in experimental peritonitis or in 12-O-tetradecanoylphorbol-13-acetate–induced edema. Overexpression of ARF, but not its downstream target p53, rescued the ARF-deficient phenotype, increasing TLR4 levels and restoring inflammatory reaction. An increase in the E2F1 protein levels observed in ARF−/− macrophages at basal condition and after LPS stimulation may be involved in the impaired response in this system, as E2F1 has been described as an inflammatory suppressor. These results indicate that tumor suppressor ARF is a new regulator of inflammatory cell signaling.

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“…The transcription factor E2F1 represses the expression of IRF-3 by directly binding to its promoter (15,16). The CCAAT̸enhancer-binding protein (C̸EBP) family of transcription factors augments proximal and distal promoter activation of LMP1 by binding to a motif in the proximal promoter (17).…”

Section: Discussionmentioning

confidence: 99%

Upregulation of a spliced variant of human interferon regulatory factor 3 through binding of the transcription factor Sp1 to the promoter

et al. 2013

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Abstract. Interferon regulatory factor 3 (IRF-3) plays an important role in host defense against viral and bacterial infection. IRF-3 includes a variety of spliced variants, which may regulate the transcription of IRF-3. We previously identified two novel IRF-3 spliced variants, Int2V1 and Int2V2, starting from intron 2 of the wild-type of IRF-3. However, the mechanism through which the IRF-3 spliced variants regulate transcription has not been elucidated. In this study, we demonstrated that the transcription factor Sp1 upregulates the basal transcriptional activity of IRF-3 Int2V1. By transient transfection analysis, we demonstrated that the overexpression of Sp1 led to positive regulation, whereas knocking down of the endogenous Sp1 resulted in repression of IRF-3 promoter activity. Electrophoretic gel mobility shift assays and chromatin immunoprecipitation assays demonstrated that Sp1 interacted with the IRF-3 promoter in vitro and in vivo. These results suggested that Sp1 positively regulated the transcription of a spliced variant of IRF-3 through directly binding to the Sp1 consensus binding site.

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Direct repression of the human IRF-3 promoter by E2F1

Cited by 17 publications

References 19 publications

Retracted: The E2F1 Oncogene Transcriptionally Regulates NELL2 in Cancer Cells

Retracted: The E2F1 Oncogene Transcriptionally Regulates NELL2 in Cancer Cells

The Tumor Suppressor ARF Regulates Innate Immune Responses in Mice

Upregulation of a spliced variant of human interferon regulatory factor 3 through binding of the transcription factor Sp1 to the promoter

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