Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Expression data from wild-type and Dazap1 mutant mouse testes

ABSTRACT: Deleted in Azoospermia Associated Protein 1 (DAZAP1) is a ubiquitous RNA-binding protein that is highly expressed in the testis. It is a component of the hnRNP particles and shuttles between the nucleus and the cytoplasm. Mice expressing the DAZAP1-Fn mutant protein manifest both growth retardation and spermatogenic arrest before meiosis I. To elucidate the biological function(s) of DAZAP1 and to search for its natural RNA substrates, we compared the expression profiles of wild-type and Dazap1 mutant testes by cDNA microarrays.

ORGANISM(S): Mus musculus

PROVIDER: GSE42601 | GEO | 2013/06/01

SECONDARY ACCESSION(S): PRJNA182339

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Expression data from wild-type and Dazap1 mutant mouse testes

Project description:Deleted in Azoospermia Associated Protein 1 (DAZAP1) is a ubiquitous RNA-binding protein that is highly expressed in the testis. It is a component of the hnRNP particles and shuttles between the nucleus and the cytoplasm. Mice expressing the DAZAP1-Fn mutant protein manifest both growth retardation and spermatogenic arrest before meiosis I. To elucidate the biological function(s) of DAZAP1 and to search for its natural RNA substrates, we compared the expression profiles of wild-type and Dazap1 mutant testes by cDNA microarrays. We used wild-type and Dazap1 mutant mouse testes. Each genotype has three replicates. 6 total samples were analyzed.

2013-06-01 | E-GEOD-42601 | biostudies-arrayexpress

The data of differentially regulated exons from mouse testes - wild-type and Dazap1 mutant

Project description:The binding of Deleted in Azoospermia Associated Protein 1 (DAZAP1) to splicing mutations in the BRCA1 and NF1 genes that caused exon exclusion suggest a role for DAZAP1 in RNA splicing. To elucidate the biological functions of DAZAP1 and to search for its natural RNA substrates, we compared the exon usages of wild-type and Dazap1 mutant testes by exon microarrays.

2013-06-01 | GSE42603 | GEO

The data of differentially regulated exons from mouse testes - wild-type and Dazap1 mutant

2013-06-01 | E-GEOD-42603 | biostudies-arrayexpress

The underlying mechanism by which DAZAP1 exerted carcinogenesis and its potential targets in MM

Project description:An RIP experiment was performed in CAG cells using FLAG antibody as bait. The position of peak summit around transcript start sites of genes can predict the interaction sites of protein and gene. We compared the peak summit of CAG EV and CAG DAZAP1 OE cells to find the differences between CAG EV cells and CAG DAZAP1 OE cells.

2024-11-01 | GSE189240 | GEO

Effect of DAZAP1 deletion on gene expression in Cal27 cell line during progression of oral squamous cell carcinoma

Project description:Tumor invasion and metastasis are the underlying cause of clinical refractoriness in oral squamous carcinoma (OSCC). Energy metabolism reprogramming has been identified as a vital process mediating tumor metastasis, indicating an urgent need for in-depth investigate into the specific mechanisms of tumor energy metabolism. Here, we identify an RNA-binding protein, DAZ associate protein 1 (DAZAP1), as a tumor-promoting factor to play an important role in OSCC progression. In vitro assays demonstrated that DAZAP1 was significantly upregulated in OSCC, while enhanced the migration and invasion of OSCC cells as well as epithelial-mesenchymal transition (EMT). RNA-seq analysis and experimental validation showed that DAZAP1 can regulate mitochondrial energy metabolism in OSCC. Mechanistically, we found that DAZAP1 underwent liquid-liquid phase separation (LLPS) to accumulate in the nucleus and enhanced cytochrome-c oxidase 16 (COX16) expression via regulating pre-mRNA alternative splicing, thereby promoted OSCC invasion and mitochondrial respiration. Finally, we observed a significant positive correlation between DAZAP1 and COX16, and high expression of these two proteins were both closely associated with poor prognosis in OSCC patients. Together, our study reveals a novel regulatory mechanism of DAZPA1 in mitochondrial metabolism and tumor development of OSCC by phase separation, suggesting the potential role of DAZAP1 in developing therapeutic strategies against OSCC invasion and metastasis.

2024-07-31 | GSE263795 | GEO

The splicing activator DAZAP1 integrates splicing control into MEK/Erk regulated cell proliferation and migration

Project description:DAZAP1 was depleted in culterd HEK 293T cells using shRNA and the resulting poly A RNA were isolated c-DNA library constructed and paired end sequenced on illumina Hi-seq 2000 platform the data was compared to a control shRNA depleted cell Gene expression and splicing switches upon DAZAP1 knockdown

2013-12-25 | E-GEOD-52745 | biostudies-arrayexpress

Next-Generation Sequencing Facilitates Quantitative Analysis of Wild Type and DAZAP1 Knockout of ESCC Transcriptomes

Project description:We aimed to detect the mRNA expression levels in KYSE510 cells after transfection with NC RNA or DAZAP1 siRNAs.

2020-04-24 | GSE134376 | GEO

Major hnRNP proteins act as general TDP-43 functional modifiers both in Drosophila and human neuronal cells.

Project description:Nuclear factor TDP-43 is known to play an important role in several neurodegenerative pathologies. In general, TDP-43 is an abundant protein within the eukaryotic nucleus that binds to many coding and non-coding RNAs and influence their processing. Using Drosophila, we have performed a functional screening to establish the ability of major hnRNP proteins to affect TDP-43 overexpression/depletion phenotypes. Interestingly, we observed that lowering hnRNP and TDP-43 expression has a generally harmful effect on flies locomotor abilities. In parallel, our study has also identified a distinct set of hnRNPs that is capable of powerfully rescuing TDP-43 toxicity in the fly eye (Hrb27c, CG42458, Glo and Syp). Most importantly, removing the human orthologs of Hrb27c (DAZAP1) in human neuronal cell lines can correct several pre-mRNA splicing events altered by TDP-43 depletion. Moreover, using RNA sequencing analysis we show that DAZAP1 and TDP-43 can co-regulate an extensive number of cellular pathways potentially important for the neuron biology. Our results suggest that changes in hnRNP expression levels can significantly modulate TDP-43 functions and affect pathological outcomes.

2017-05-31 | GSE97262 | GEO

The splicing activator DAZAP1 integrates splicing control into MEK/Erk regulated cell proliferation and migration

2013-12-25 | GSE52745 | GEO

HNRNPA2B1 regulates alternative RNA processing in the nervous system and accumulates in granules in ALS IPSC-derived motor neurons [hnRNPA2B1_Arrays_mouse_SC]

Project description:HnRNPA2B1 encodes an RNA binding protein associated with neurodegenerative disorders. However, its function in the nervous system is unclear. Transcriptome-wide cross-linking and immunoprecipitation in mouse spinal cord discover UAGG motifs enriched within ~2,500 hnRNP A2/B1 binding sites and an unexpected role for hnRNP A2/B1 in alternative polyadenylation. Loss of hnRNP A2/B1 results in alternative splicing, including skipping of an exon in amyotrophic lateral sclerosis (ALS)-associated D-amino acid oxidase (DAO) that reduces D-serine metabolism. Inclusion of the DAO exon is also reduced in transgenic ALS mice models. ALS-associated hnRNP A2/B1 D290V mutant patient fibroblasts and motor neurons differentiated from induced pluripotent stem cells demonstrate gain-of-mutant-dependent splicing differences. Mutant motor neurons also exhibit increased hnRNP A2/B1 localization to cytoplasmic granules during stress, which are abrogated by a small molecule CA43. Our findings and cellular resource identify RNA networks affected in loss of normal and mutated hnRNP A2/B1 with broad relevance to neurodegeneration.

2016-10-20 | GSE86224 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data