Homo sapiens
Ontology highlight
ABSTRACT:
OTHER RELATED OMICS DATASETS IN: E-GEOD-53470
PROVIDER: PRJNA232070 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR1054670.fastq.gz | Fastqsanger.gz | |||
| SRR1054671.fastq.gz | Fastqsanger.gz | |||
| SRR1054672.fastq.gz | Fastqsanger.gz | |||
| SRR1054673.fastq.gz | Fastqsanger.gz | |||
| SRR1054674.fastq.gz | Fastqsanger.gz |
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Similar Datasets
Project description:In our investigations of the molecular pathways of prostate tumorigenesis in Nkx3.1; Pten mutant mice using gene expression profiling, we now find that the AP-1 transcription factors, c-Jun and c-Fos, are significantly up-regulated during cancer progression. Forced expression of c-Fos and c-Jun in prostate cancer cells results in increased tumorigenicity, activation of Erk MAP kinase, and enhanced survival in the absence of androgens, which are hallmarks of disease progression. In humans, Jun and Fos proteins are significantly up-regulated during prostate cancer progression and significantly correlated with activation of Erk MAP kinase. Most notably, expression of Jun is associated with disease recurrence independent of other currently used prognostic indicators. These analyses reveal a hitherto unappreciated role for AP-1 transcription factors in prostate cancer progression vis-à-vis Erk MAP kinase signaling, as well as the identification of a novel marker of disease recurrence, namely c-Jun. Keywords: Stages of Prostate Cancer
2008-06-27 | GSE11836 | GEO
Project description:In our investigations of the molecular pathways of prostate tumorigenesis in Nkx3.1; Pten mutant mice using gene expression profiling, we now find that the AP-1 transcription factors, c-Jun and c-Fos, are significantly up-regulated during cancer progression. Forced expression of c-Fos and c-Jun in prostate cancer cells results in increased tumorigenicity, activation of Erk MAP kinase, and enhanced survival in the absence of androgens, which are hallmarks of disease progression. In humans, Jun and Fos proteins are significantly up-regulated during prostate cancer progression and significantly correlated with activation of Erk MAP kinase. Most notably, expression of Jun is associated with disease recurrence independent of other currently used prognostic indicators. These analyses reveal a hitherto unappreciated role for AP-1 transcription factors in prostate cancer progression vis-à -vis Erk MAP kinase signaling, as well as the identification of a novel marker of disease recurrence, namely c-Jun. Experiment Overall Design: Mouse prostate was collected from wild-type or the Nkx3.1; Pten compound mutant mice at the age of 8-16 months. One lobe of dosolateral prostate was snap-frozen in OCT and stored at -80ºC for laser capture microdissection (LCM). To obtain androgen-independent lesions, mice were castrated at 7 to 14 months of age. Mice were sacrificed for analysis at 8 to 16 months of age and one dosolateral prostatic lobe was snap-frozen in OCT and stored at -80ºC for LCM. Approximate 1000 Prostate epithelial cells were isolated from normal prostate, dysplasia, prostatic intraepithelial neoplasia (PIN) or cancer lesions using PixCell IIE LCM system (Arcturus), followed by RNA linear amplification and labeling using Small Sample Labeling Protocol VII (Affymetrix). Samples were labeled using a BioArray High Yield RNA transcript labeling kit (Enzo Life Scientific) and were hybridized to MOE430A GeneChips containing 22,690 well characterized mouse genes/ESTs (Affymetrix).
2008-10-21 | E-GEOD-11836 | biostudies-arrayexpress
Project description:Reiterer2013 - pseudophosphatase STYX role in
ERK signalling
This model is described in the article:
Pseudophosphatase STYX
modulates cell-fate decisions and cell migration by
spatiotemporal regulation of ERK1/2.
Reiterer V, Fey D, Kolch W,
Kholodenko BN, Farhan H.
Proc. Natl. Acad. Sci. U.S.A. 2013 Jul;
110(31): E2934-43
Abstract:
Serine/threonine/tyrosine-interacting protein (STYX) is a
catalytically inactive member of the dual-specificity
phosphatases (DUSPs) family. Whereas the role of DUSPs in
cellular signaling is well explored, the function of STYX is
still unknown. Here, we identify STYX as a spatial regulator of
ERK signaling. We used predictive-model simulation to test
several hypotheses for possible modes of STYX action. We show
that STYX localizes to the nucleus, competes with nuclear DUSP4
for binding to ERK, and acts as a nuclear anchor that regulates
ERK nuclear export. Depletion of STYX increases ERK activity in
both cytosol and nucleus. Importantly, depletion of STYX causes
an ERK-dependent fragmentation of the Golgi apparatus and
inhibits Golgi polarization and directional cell migration.
Finally, we show that overexpression of STYX reduces ERK1/2
activation, thereby blocking PC12 cell differentiation.
Overall, our results identify STYX as an important regulator of
ERK1/2 signaling critical for cell migration and PC12 cell
differentiation.
This model is hosted on
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and identified by:
BIOMD0000000557.
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BioModels Database:
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To the extent possible under law, all copyright and related or
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2024-09-02 | BIOMD0000000557 | BioModels
Project description:ETS1 and RAS/ERK regulate a common gene expression program in establishing enviroment suitable for prostate cancer cell migration. ChIP-sequencing of various transcription factors
2014-10-07 | E-GEOD-59021 | biostudies-arrayexpress
Project description:Prostate cancer morbidity and mortality obviate a need for more effective targeted therapies. One potential target is EphA2, although paradoxically, pro- and anti-oncogenic effects have been shown to be mediated by EphA2. We demonstrate that unique activating and blocking EphA2-targeting monoclonal antibodies display opposing tumor-suppressive and oncogenic properties in vivo. To further explore this complexity, we performed detailed phosphoproteomic analysis following ligand-induced EphA2 activation. Our analysis identified altered phosphorylation of 73 downstream proteins related to the PI3K/AKT/mTOR and ERK/MAPK pathways, with the majority implicated in cell junction and cytoskeletal organization, cell motility, and tumor metastasis. We demonstrate that the adaptor protein SHB is an essential component in mediating the inhibition of the Erk/MAPK pathway in response to EphA2 receptor activation. Furthermore, we identify the adherence junction protein afadin as an EphA2-regulated phosphoprotein which is involved in prostate cancer migration and invasion.
2024-11-11 | PXD053835 | Pride
Project description:Marekâs disease (MD) is an economically significant disease in chickens caused by the highly oncogenic Marekâs disease virus (MDV). A major unanswered question is the mechanism of MDV-induced tumor formation. Meq, a bZIP transcription factor discovered in the 1990s, is critically involved in viral oncogenicity but only a few of its host target genes have been described impeding our understanding of MDV-induced tumorigenesis. Using ChIP-seq and microarray analysis, a high confidence list of Meq-binding sites in the chicken genome and a global transcriptome of Meq-responsive genes was generated. Meq binding sites were found to be enriched in the promoter regions of up-regulated genes, but not in those of down-regulated genes. ChIP-seq was also performed for c-Jun, a known heterodimeric partner of Meq. Close location of binding sites of Meq and c-Jun was noted, suggesting cooperativity between these two factors in modulating transcription. Pathway analysis indicated that Meq transcriptionally regulates many genes that are part of several signaling pathways include the ERK/MAPK, Jak-STAT, and ErbB pathways that are critical for oncogenesis and/or include signaling mediators involved in apoptosis. Meq activates oncogenic signaling cascades by transcriptionally activating major kinases in the ERK/MAPK pathway and simultaneously repressing phosphatases, as verified using inhibitors of MEK and ERK1/2 in a cell proliferation assay. This study provides significant insights into the mechanistic basis of Meq-dependent cell transformation. ChiP-Seq of Meq-DF-1 clone 5G (DF-1 stably expressing Meq driven by the CMV promoter) with Meq and Jun antibodies
2016-07-01 | E-GEOD-48451 | biostudies-arrayexpress
Project description:Knockdowns of c-JUN and JUND had opposite effects on PC3 prostate cell migration. We predicted that c-JUN and JUND control the same set of cell migration genes, but in opposite directions. To test this hypothesis, mRNA with expression changes in c-JUN and JUND knockdown PC3 cell lines were compared to mRNA levels in control (luciferase knockdown) PC3 cells by RNA-seq. mRNA profiles of luciferase knockdown (WT), c-Jun knockdown, and Jun-D knockdown in PC3 cells were generated using deep sequencing, in triplicate, using Illumina HiSeq. Knockdowns were stable shRNA expression from a lentiviral construct selected with puromycin.
2014-10-23 | E-GEOD-53470 | biostudies-arrayexpress
Project description:Knockdowns of c-JUN and JUND had opposite effects on PC3 prostate cell migration. We predicted that c-JUN and JUND control the same set of cell migration genes, but in opposite directions. To test this hypothesis, mRNA with expression changes in c-JUN and JUND knockdown PC3 cell lines were compared to mRNA levels in control (luciferase knockdown) PC3 cells by RNA-seq.
2014-10-23 | GSE53470 | GEO
Project description:Approximately 50% of prostate cancers have chromosomal translocations resulting in the over-expression one of four ETS family transcription factors. However, it is not known why these four four family members are selected for oncogenic roles, while other ETS proteins are not. We found that the four oncogenic ETS family members have a specific role in prostate cell migration. Using chromatin immunoprecipitation coupled with next-generation sequencing, this specific biological function was matched to a specific set of genomic targets highlighted by the presence of an AP-1 binding site. ETS/AP-1 binding sites are prototypical Ras-responsive elements, but oncogenic ETS proteins could activate a Ras/MAPK transcriptional program in the absence of MAPK activation. These findings indicate that the specific function of ETS proteins over-expressed in prostate cancer is the activation of a Ras/MAPK gene expression program in the absence of signaling pathway mutations. ChIP sequencing two transcription factors in PC3 cells, four transcription factors plus a FLAG control in RWPE-1 cells and input DNA sequencing from each cell line.
2011-10-19 | E-GEOD-29808 | biostudies-arrayexpress
Project description:The p53-family member p73 functions in various cellular signaling pathways and can have tumor suppressor properties. Several isoforms of p73 exist that differ considerably in their function. Whereas the functions of the N-terminal isoforms (TA and M-NM-^TNp73) and their opposing pro- and anti-apoptotic roles became evident, the functional differences of the distinct C-terminal spliceforms of TAp73 have remained unclear. Here, we characterized the genomic binding sites for TAp73M-NM-1 and TAp73M-NM-2 and identified a specific p73 consensus binding-motif. Furthermore, an AP1 motif is strongly enriched close to binding sites for TAp73M-NM-1. These AP1 motif-containing target genes are selectively upregulated by TAp73M-NM-1, while their mRNA expression is repressed upon TAp73M-NM-2 induction. Recruitment of c-Jun to the respective AP1 sites was impaired upon TAp73M-NM-2 expression in part due to downregulation of c-Jun. We show that several of these AP1-site containing TAp73M-NM-1-induced genes reduce on apoptosis-induction suggesting an underlying molecular mechanism for the observed functional differences between TAp73M-NM-1 and TAp73M-NM-2. ChIP-seq and RNA-seq profiles of TAp73alpha, TAp73beta and p53 stably transfected in human osteosarcoma Saos cells
2011-03-01 | E-GEOD-15780 | biostudies-arrayexpress