Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The inhibition of m6A modification on reporter mRNA by STM2457

ABSTRACT: We present a spatiotemporal m6A imaging system (SMIS) that can monitor the m6A modification and the translation of mRNAs with high specificity and sensitivity in a single live cell. The SMIS system contains a m6A-modified reporter mRNA and fluorescence resonance energy transfer (FRET) biosensors. To quantify the methylation viariation achieved at m6A sites in the reporter mRNA after STM2457 treatment, a classical METTL3 inhibitor, we performed m6ACE-seq to measure the relative m6A level with single-base-resolusion.

ORGANISM(S): Homo sapiens

PROVIDER: GSE273366 | GEO | 2024/10/11

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

the inhibition of m6A modification on reporter mRNA by STM2457

Project description:the inhibition of m6A modification on reporter mRNA by STM2457

| PRJNA1141493 | ENA

RNA-seq of human breast cancer cell line MDA-MB-231 treated with STM2457 against untreated controls

Project description:Here, we aim to investigate if catalytic inhibition of the m6A methyltransferase METTL3 by the small-molecule STM2457 may be a viable treatment option for TNBC.

2023-12-18 | E-MTAB-13184 | biostudies-arrayexpress

Small-molecule Inhibition of METTL3 Suppresses Tumor Growth and Promotes Neuroblastoma Differentiation [RNA-Seq STM]

Project description:The N6-methyladenosine (m6A) RNA modification is an important regulator of gene expression. m6A is deposited by a methyltransferase complex that includes methyltransferase-like 3 (METTL3) and methyltransferase-like 14 (METTL14). High levels of METTL3 and METTL14 drive the growth of many types of adult cancer, and METTL3/METTL14 inhibitors are emerging as new anticancer agents. However, little is known about the m6A epitranscriptome or the role of the METTL3/METTL14 complex in neuroblastoma, a common pediatric cancer. Here, we show that METTL3 knockdown or pharmacologic inhibition with the small molecule STM2457 leads to reduced neuroblastoma cell proliferation and increased differentiation. These changes in neuroblastoma phenotype were associated with decreased m6A deposition on transcripts involved in nervous system development and neuronal differentiation and increased stability and expression of target mRNAs. In preclinical studies, STM2457 treatment suppressed the growth of neuroblastoma tumors in vivo. Together, these results support the potential of METTL3/METTL14 complex inhibition as therapeutic strategy against neuroblastoma.

2024-04-10 | GSE262731 | GEO

Small-molecule Inhibition of METTL3 Suppresses Tumor Growth and Promotes Neuroblastoma Differentiation [meRIP-Seq]

2024-04-10 | GSE240582 | GEO

Small-molecule Inhibition of METTL3 Suppresses Tumor Growth and Promotes Neuroblastoma Differentiation [RNA-Seq Decay]

2024-04-10 | GSE240581 | GEO

Small-molecule Inhibition of METTL3 Suppresses Tumor Growth and Promotes Neuroblastoma Differentiation [RNA-seq siMETTL3]

2024-04-10 | GSE263118 | GEO

DARTseq identifies m6A targets in human CD34+ HSPCs

Project description:The goal of this study is to identify m6A targets in human CD34+ HSPCs with or without STM2457 treatment using DARTseq. Purified human CD34+ HSPC cells were transduced with APOBEC-YTH or empty vector control (MIG). 24hr post infection, CD34+ cells were treated with STM2457 at a concentration of 20µM for 2 days. GFP+ cells were sorted the next day. 3 replicates were performed.

2023-12-07 | GSE231861 | GEO

GNPS Mono-Colonized GF Reporter Mice

Project description:Mono-colonized GF reporter mice fecal metabolomics by LC-MS/MS

2021-08-31 | MSV000088040 | GNPS

Interaction partners of arginyl-tRNA protein transferase in the moss Physcomitrella patens

Project description:Protein arginylation is a post-translational modification at the N-terminus of proteins and is crucial for viability and physiology in higher eukaryotes. The lack of arginylation causes severe developmental defects in plants and embryo lethality in Drosophila and in mice. Although several studies investigated impact and function of the responsible enzyme, the arginyl-tRNA protein transferase (ATE) in plants, identification of arginylated proteins by mass spectrometry was not hitherto achieved. In the present study, we report the identification of targets and interaction partners of ATE in the model plant Physcomitrella patens by mass spectrometry employing two different immuno-affinity strategies and a recently established transgenic ATE:GUS reporter line (Schuessele et al., 2015 New Phytol., DOI: 10.1111/nph.13656). Here we use a commercially available antibody against the fused reporter protein (GUS) to pull down ATE and its interacting proteins and validate the in vivo interaction with a class I small heatshock protein via Förster resonance energy transfer (FRET).

2016-04-19 | PXD003228 | Pride

m6A and YTHDF proteins control the subcellular localization of select neuronal mRNAs [RNA-seq and DART-seq]

Project description:The transport of mRNAs to distal subcellular compartments is an important component of spatial gene expression control in neurons. However, the mechanisms that control mRNA localization in neurons are not completely understood. Here, we identify the abundant base modification, m6A, as a regulator of mRNA localization in neurons. Transcriptome-wide analysis of mRNA localization in neurons following genetic loss of m6A reveals hundreds of transcripts that exhibit altered subcellular localization. Additionally, using a reporter system, we show that mutation of specific m6A sites in select neuronal transcripts diminishes their localization to neurites. Single molecule fluorescent in situ hybridization experiments further confirm our findings and identify the m6A reader proteins YTHDF2 and YTHDF3 as mediators of this effect. Our findings reveal a novel function for m6A in controlling mRNA localization in neurons and enable a better understanding of the mechanisms through which m6A influences gene expression in the brain.

2022-04-26 | GSE171199 | 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