Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Expression data of embryonic stem (ES) cells from both control and Prmt6 overexpressed population

ABSTRACT: ES cells are able to self-renew and remain pluripotent. These characteristics are maintained by both genetic and epigenetic regulators. Protein arginine methyltransferase (PRMT) 4 and 5 are shown to be important in early embryonic development and in ES cells. PRMT6-mediated di-methylation of histone H3 at arginine 2 (H3R2me2) can antagonize the tri-methylation of histone H3 at lysine 4, which marks active genes. However, it is unclear whether PRMT6 and PRMT6-mediated H3R2me2 play crucial roles in early embryonic development and ES cell identity. In this study, we investigate their functions using mouse ES cells as the model. We used microarray (Affymetrix GeneChip Mouse Gene 1.0ST) to examine the global change of gene expression in mouse ES cells when Prmt6 was overexpressed and identified distinct classes of genes that are up-regulated and down-regulated during this process.

ORGANISM(S): Mus musculus

PROVIDER: GSE27685 | GEO | 2011/03/04

SECONDARY ACCESSION(S): PRJNA138163

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Expression data of embryonic stem (ES) cells from both control and Prmt6 overexpressed population

Project description:ES cells are able to self-renew and remain pluripotent. These characteristics are maintained by both genetic and epigenetic regulators. Protein arginine methyltransferase (PRMT) 4 and 5 are shown to be important in early embryonic development and in ES cells. PRMT6-mediated di-methylation of histone H3 at arginine 2 (H3R2me2) can antagonize the tri-methylation of histone H3 at lysine 4, which marks active genes. However, it is unclear whether PRMT6 and PRMT6-mediated H3R2me2 play crucial roles in early embryonic development and ES cell identity. In this study, we investigate their functions using mouse ES cells as the model. We used microarray (Affymetrix GeneChip Mouse Gene 1.0ST) to examine the global change of gene expression in mouse ES cells when Prmt6 was overexpressed and identified distinct classes of genes that are up-regulated and down-regulated during this process. Mouse ES cells were transfected with either pCAGIP.puro empty vector (control) or Prmt6 overexpressing plasmid (P+6 OE). After 3 days of selection by puromycin, cells from both populations were subjected to RNA extraction and hybridization on Affymetrix microarrays.

2011-03-04 | E-GEOD-27685 | biostudies-arrayexpress

PRMT6 substrate specificity analysis

Project description:Protein arginine methyltransferase 6 (PRMT6) catalyses the asymmetric dimethylation of arginines on numerous substrate proteins within the human cell. In particular, PRMT6 methylates histone H3 arginine 2 (H3R2) which affects both gene repression and activation. However, the substrate specificity of PRMT6 has not been comprehensively analysed. Here we have systematically characterised the substrate recognition motif of PRMT6 in context of the histone H3 tail, finding that it has broad specificity and recognises the RG motif. Working with a H3 tail peptide as a template, on which we made 204 amino acid substitutions, we use targeted mass spectrometry to measure the effect on PRMT6 in vitro activity. We first show that PRMT6 methylates R2 and R8 in the H3 peptide, although H3R8 is methylated with lower efficiency and is not an in vivo PRMT6 substrate. Then, using parallel reaction monitoring (PRM) with electron transfer dissociation (ETD), we quantify the effect of 194 of these amino acid substitutions on methylation at both H3R2 and H3R8. In both cases, we find that PRMT6 is capable of tolerating essentially any amino acid substitution in the H3 peptide, but that positively charged and bulky residues are preferred near the target arginine. We show that PRMT6 prefers glycine in the position immediately following the target arginine, indicating that PRMT6 recognises the RG motif. We confirm this preference for the RG motif on another PRMT6 substrate, histone H4R3. This broad specificity, along with recognition of RG rather than RGG, is distinctive among the PRMT family and has implications for the development of drugs to selectively target PRMT6.

2021-03-31 | PXD016711 | panorama

Genomic occurrence analysis of PRMT6-dependent H3R2me2a

Project description:Protein arginine methyltransferase 6 (PRMT6) is an epigenetic regulator of fundamental cellular processes, such as gene expression and DNA repair. Asymmetric dimethylation of histone H3 at arginine 2 (H3R2me2a) is the major histone modification catalyzed by PRMT6. To identify the genome-wide deposition and transcriptional impact of H3R2me2a, we established PRMT6 deletion in a human cell model of neural differentiation. These knockout cells show severe neural differentiation defects. ChIP-seq profiling reveals that H3R2me2a is present at promoter as well as non-promoter sites in a PRMT6-dependent manner. Loss of H3R2me2a causes enhanced H3K4me3 deposition and target gene transcription supporting a genome-wide repressive nature of H3R2me2a. Intriguingly, the non-promoter H3R2me2a peaks co-localize with active enhancer marks, such as H3K4me1 and H3K27ac.

2018-09-27 | GSE107609 | GEO

Repressive mark H3K27me3 in PRMT6 KO NT2/D1 cells

2018-09-27 | GSE117341 | GEO

Genomic location of PRMT6-dependent H3R2 methylation is decisive for the transcriptional outcome of associated genes [ChIP-seq]

2018-09-27 | GSE117200 | GEO

PRMT6-CDC20 facilitates glioblastoma progression via the degradation of CDKN1B

Project description:PRMT6, a type I arginine methyltransferase, di-methylates the arginine residues of both histones and non-histones asymmetrically. Increasing evidence indicates that PRMT6 plays a tumor mediator involved in human malignancies. Here, we aim to uncover the essential role and underlying mechanisms of PRMT6 in promoting glioblastoma (GBM) proliferation. Investigation of PRMT6 expression in glioma tissues demonstrated that PRMT6 is overexpressed, and elevated expression of PRMT6 is negatively correlated with poor prognosis in glioma/GBM patients. Silencing PRMT6 inhibited GBM cell proliferation and induced cell cycle arrest at the G0/G1 phase, while overexpressing PRMT6 had opposite results. Further, we found that PRMT6 attenuates the protein stability of CDKN1B by promoting its degradation. Subsequent mechanistic investigations showed that PRMT6 maintains the transcription of CDC20 by activating histone methylation mark (H3R2me2a), and CDC20 interacts with and destabilizes CDKN1B. Rescue experimental results confirmed that PRMT6 promotes the ubiquitinated degradation of CDKN1B and cell proliferation via CDC20. We also verified that the PRMT6 inhibitor (EPZ020411) could attenuate the proliferative effect of GBM cells. Our findings illustrate that PRMT6, an epigenetic mediator, promotes CDC20 transcription via H3R2me2a to mediate the degradation of CDKN1B to facilitate GBM progression. Targeting PRMT6-CDC20-CDKN1B axis might be a promising therapeutic strategy for GBM.

2023-03-31 | GSE221971 | GEO

Asymmetric demethylation at histone H3 arginine 2 by PRMT6 in gastric cancer progression (NUGC3 cell line)

Project description:Purpose: Dysregulation of histone H3 arginine (R) methylation is still unknown in primary cancer including gastric cancer (GC), although PRMT6 plays a role in asymmetric dimethylation at H3R2 (H3R2me2as) in cancer cells. The objective is to clarify biological and molecular roles of H3R2me2as-PRMT6 pathway in GC. Experimental Design: We assessed H3R2me2as and PRMT6 levels in 133 primary GC tissues by immunohistochemistry. We analyzed biological functions of PRMT6 in GC cell lines using a lentivirus overexpression and CRISPR/Cas9-based knockout of PRMT6 systems. Results: Increased H3R2me2as was found in 68 GC (51.1%) cases and independently correlated with poor prognosis. PRMT6 was overexpressed in 70 (52.6%) GC, which strongly correlated with the H3R2me2as levels (P<0.001). PRMT6 overexpression in GC cells enhanced global H3R2me2as levels, cell invasiveness in vitro, while PRMT6-knockout GC cells suppressed these effects. PRMT6 knockout also impaired tumorigenicity in vivo. Microarray and ChIP assays demonstrated that PRMT6-knockout GC cells decreased the H3R2me2as levels at the promoter regions of PCDH7, SCD and IGFBP5, resulting in up-reregulation of their gene expression. PRMT6 recruited at the regions of PCDH7 and SCD in the PRMT6-overexpressed cells. Knockdown of tumor suppressor PCDH7 in PRMT6-knockout GC cells elevated cell migration and invasion. PRMT6 expression inversely correlated with PCDH7 expression in primary GC (P=0.021). Conclusions: H3R2me2as is a strong prognostic indicator of GC patients. Global and gene-specific H3R2me2as are maintained by PRMT6. PRMT6-overexpressed GC cells may acquire invasiveness through direct inhibition of PCDH7 by increasing H3R2me2as activity. Thus, PRMT6-H3R2me2as pathway is a promising new therapeutic target in GC.

2020-04-16 | GSE113189 | GEO

Asymmetric demethylation at histone H3 arginine 2 by PRMT6 in gastric cancer progression (AGS cell line)

2020-04-16 | GSE113188 | GEO

Asymmetric demethylation at histone H3 arginine 2 by PRMT6 in gastric cancer progression

Project description:Asymmetric demethylation at histone H3 arginine 2 by PRMT6 in gastric cancer progression

| PRJNA450398 | ENA

Dynamics of m6A RNA methylome during leukemogenesis reveals a role of IGF2BP2-PRMT6-MFSD2A signaling axis in maintaining AML stem cells [Prmt6 RNA-seq]

Project description:Our data reveal that RNA m6A displays a sharp transition during leukemogenesis and involves in acquiring stem cell properties of leukemia stem cells (LSCs). We find that m6A reader IGF2BP2 and protein arginine methyltransferase PRMT6 play key roles in the acquisition of LSCs properties. Genetical deletion and pharmacological inhibition of PRMT6 delayed AML development. Mechanistically, IGF2BP2 regulates PRMT6 expression by stabilizing its mRNA in an m6A-dependent manner. PRMT6 further suppresses the expression of lipid transporter MFSD2A by establishing inactive H3R2me2a in its promoter region. Loss of PRMT6 and IGF2BP2 upregulates the expression of MFSD2A that increases the uptake of docosahexaenoic acid. Collectively, our findings uncover a critical role of IGF2BP2-PRMT6-MFSD2A signaling axis in AML development, and provide a promising therapeutic strategy for targeting LSCs.

2023-06-20 | GSE210279 | 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